Protein Structure and Engineering

Proceedings of the Tenth Course of the International School of Pure and Applied Biostructure (Erice, Italy, June 1989). Knowledge of protein structure and of design and manufacture methods has made it possible to produce proteins of any desired sequence, but progress is limited by inability to predi

[1]  C. Walsh,et al.  Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide. , 1982, The Journal of biological chemistry.

[2]  L. Kay,et al.  Three-Dimensional Heteronuclear NMR of 15 N-Labeled Proteins , 2022 .

[3]  Richard Earl Dickerson,et al.  Hemoglobin : structure, function, evolution, and pathology , 1983 .

[4]  J. LEE,et al.  Nuclear Magnetic Resonance , 1968, Nature.

[5]  D. Powers,et al.  In vivo formation and stability of engineered disulfide bonds in subtilisin. , 1986, The Journal of biological chemistry.

[6]  W. Bialek,et al.  Do vibrational spectroscopies uniquely describe protein dynamics? The case for myoglobin. , 1985, Biophysical journal.

[7]  Ronald M. Levy,et al.  Molecular dynamics of an a-helical polypeptide: Temperature dependence and deviation from harmonic behavior (protein dynamics/temperature factor/quantum corrections/fluctuations/normal modes) , 1982 .

[8]  A. Cooper.  Dynamics of Proteins and Nucleic Acids , 1988 .

[9]  I. Solomon.  Relaxation Processes in a System of Two Spins , 1955 .

[10]  I. R. Mcdonald,et al.  Theory of simple liquids , 1998 .

[11]  E. M.,et al.  Statistical Mechanics , 2021, Manual for Theoretical Chemistry.

[12]  W. M. Westler,et al.  Two-dimensional NMR approaches to the study of protein structure and function. , 1984, Federation proceedings.

[13]  K. Moffat,et al.  The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins. , 1986, The Journal of biological chemistry.

[14]  K. Wüthrich,et al.  Carbon‐13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐ X‐L‐ Ala‐OH , 1978 .

[15]  T. Grundström,et al.  Expression of bovine intestinal calcium binding protein from a synthetic gene in Escherichia coli and characterization of the product. , 1986, Biochemistry.

[16]  Terrence G. Oas,et al.  A peptide model of a protein folding intermediate , 1988, Nature.

[17]  P. Karplus,et al.  Refined structure of glutathione reductase at 1.54 A resolution. , 1987, Journal of molecular biology.

[18]  E. Haas,et al.  Estimation of intramolecular distance distributions in bovine pancreatic trypsin inhibitor by site-specific labeling and nonradiative excitation energy-transfer measurements. , 1987, Biochemistry.

[19]  M. Uziel,et al.  REACTION OF BOVINE PANCREATIC RIBONUCLEASE A WITH 1,5-DIFLUORO-2,4-DINITROBENZENE. II. STRUCTURE OF AN INTRAMOLECULARLY BRIDGED DERIVATIVE. , 1965, The Journal of biological chemistry.

[20]  J. Markley.  High-resolution proton magnetic resonance spectroscopy of selectively deuterated enzymes. , 1972, Methods in enzymology.

[21]  Structure and dynamics of detergent-solubilized M13 coat protein (an integral membrane protein) determined by 13C and 15N nuclear magnetic resonance spectroscopy. , 1990, Biochemistry and cell biology = Biochimie et biologie cellulaire.

[22]  I. Yamazaki,et al.  Diffusion effect on excitation energy transfer in solution: Analysis by means of picosecond time-resolved fluorimeter , 1985 .

[23]  N. Scrutton,et al.  Engineering of an intersubunit disulphide bridge in glutathione reductase from Escherichia coli , 1988, FEBS letters.

[24]  W C Johnson,et al.  Information content in the circular dichroism of proteins. , 1981, Biochemistry.

[25]  J. H. Noggle.  The nuclear Overhauser effect , 1971 .

[26]  S. Opella,et al.  Detection of 1H homonuclear NOE between amide sites in proteins with 1H15N heteronuclear correlation spectroscopy , 1989 .

[27]  R. Kaptein,et al.  Nonselective three-dimensional nmr spectroscopy. The 3D NOE-HOHAHA experiment , 1988 .

[28]  A. Bacher,et al.  Riboflavin synthases of Bacillus subtilis. Purification and properties. , 1980, The Journal of biological chemistry.

[29]  S. Fesik,et al.  Amide proton exchange rates of a bound pepsin inhibitor determined by isotope-edited proton NMR experiments. , 1987, Biochemical and biophysical research communications.

[30]  A. Bax,et al.  Optimization of two-dimensional homonuclear relayed coherence transfer NMR spectroscopy , 1985 .

[31]  M. Laskowski,et al.  Soybean trypsin inhibitor (Kunitz) and its complex with trypsin. Carbon-13 nuclear magnetic resonance studies of the reactive site arginine. , 1980, Biochemistry.

[32]  D. Parry,et al.  α-Helical coiled coils — a widespread motif in proteins , 1986 .

[33]  Benno P. Schoenborn,et al.  Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin , 1981, Nature.

[34]  C. Dobson,et al.  Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. , 1988, Biochemistry.

[35]  L. J. Perry,et al.  Disulfide bonds and thermal stability in T4 lysozyme. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[36]  P G Schultz,et al.  A general method for site-specific incorporation of unnatural amino acids into proteins. , 1989, Science.

[37]  H. Lipson.  Crystal Structures , 1949, Nature.

[38]  R. Griffey,et al.  Proton NMR measurements of bacteriophage T4 lysozyme aided by 15N isotopic labeling: structural and dynamic studies of larger proteins. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[39]  A. Gronenborn,et al.  Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP+ complex. , 1984, Biochemistry.

[40]  Michael Levitt,et al.  Refinement of Large Structures by Simultaneous Minimization of Energy and R Factor , 1978 .

[41]  P. Karplus,et al.  A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution. , 1989, European journal of biochemistry.

[42]  R. Schirmer,et al.  Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. , 1982, European journal of biochemistry.

[43]  Kurt Wüthrich,et al.  Stereospecific assignment of the methyl 1H NMR lines of valine and leucine in polypeptides by nonrandom 13C labelling , 1989 .

[44]  P. Model,et al.  Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. , 1988, The Journal of biological chemistry.

[45]  S. Walter Englander,et al.  Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR , 1988, Nature.

[46]  L. Bonewald,et al.  A naturally occurring structural variant of human growth hormone. , 1978, The Journal of biological chemistry.

[47]  A. Szabó,et al.  Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity , 1982 .

[48]  L. Verlet.  Computer "Experiments" on Classical Fluids. I. Thermodynamical Properties of Lennard-Jones Molecules , 1967 .

[49]  R. Woody.  Aromatic side‐chain contributions to the far ultraviolet circular dichroism of peptides and proteins , 1978 .

[50]  A. Jones,et al.  Biosynthetic 20-kilodalton methionyl-human growth hormone has diabetogenic and insulin-like activities. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[51]  M Karplus,et al.  Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism. , 1983, Journal of molecular biology.

[52]  W. D. Phillips,et al.  Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonance. , 1967, Journal of the American Chemical Society.

[53]  J M Burridge,et al.  Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim. , 1985, The Journal of biological chemistry.

[54]  R. Griffey,et al.  Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution , 1987, Quarterly Reviews of Biophysics.

[55]  R. Perham,et al.  The lipoamide dehydrogenase component of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli. , 1978, Biochemical Society transactions.

[56]  J. Kirkwood,et al.  The Radial Distribution Function in Liquids , 1942 .

[57]  V. Bystrov.  Spin—spin coupling and the conformational states of peptide systems , 1976 .

[58]  M. Karplus,et al.  Crystallographic R Factor Refinement by Molecular Dynamics , 1987, Science.

[59]  H. Rüterjans,et al.  Nuclear magnetic resonance investigation of 15N-labeled histidine in aqueous solution. , 1977, Journal of the American Chemical Society.

[60]  F. Winkler,et al.  Crystal structure of human dihydrofolate reductase complexed with folate. , 1988, European journal of biochemistry.

[61]  P. Wright,et al.  Complete assignment of the 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Application of an integrated approach to spin system identification in proteins. , 1988, Journal of molecular biology.

[62]  J T Yang,et al.  Calculation of protein conformation from circular dichroism. , 1986, Methods in enzymology.

[63]  P. Wright,et al.  Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin. , 1985, Biochimica et biophysica acta.

[64]  J. Anglister,et al.  NMR technique for assessing contributions of heavy and light chains to an antibody combining site , 1985, Nature.

[65]  M Karplus,et al.  X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution. , 1986, Journal of molecular biology.

[66]  E. Southern.  Detection of specific sequences among DNA fragments separated by gel electrophoresis. , 1975, Journal of molecular biology.

[67]  M. Kainosho,et al.  Local structural features around the C-terminal segment of Streptomyces subtilisin inhibitor studied by carbonyl carbon nuclear magnetic resonances three phenylalanyl residues. , 1987, Biochemistry.

[68]  L. Retegui,et al.  The intriguing nature of the multiple actions of growth hormone , 1979 .

[69]  A. J. Shaka,et al.  An improved sequence for broadband decoupling: WALTZ-16 , 1983 .

[70]  P. Wright,et al.  Site-selective observation of nuclear Overhauser effects in proteins via isotopic labeling , 1987 .

[71]  M Karplus,et al.  Estimation of uncertainties in X‐ray refinement results by use of perturbed structures , 1987, Proteins.

[72]  A. Gronenborn,et al.  Determination of the secondary structure of the DNA binding protein Ner from phage Mu using 1H homonuclear and 15N-1H heteronuclear NMR spectroscopy. , 1989, Biochemistry.

[73]  B. Sykes,et al.  Backbone dynamics of a model membrane protein: measurement of individual amide hydrogen-exchange rates in detergent-solubilized M13 coat protein using 13C NMR hydrogen/deuterium isotope shifts. , 1987, Biochemistry.

[74]  Thomas A. Weber,et al.  Hidden structure in liquids , 1982 .

[75]  R. L. Baldwin,et al.  Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange. , 1979, Journal of molecular biology.

[76]  C. Ho,et al.  19F NMR Investigations of Membranes , 1985 .

[77]  J. Feeney,et al.  Trimethoprim binding to Lactobacillus casei dihydrofolate reductase: a 13C NMR study using selectively 13C-enriched trimethoprim. , 1986, Biochemistry.

[78]  E. Purcell,et al.  Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments , 1954 .

[79]  D. G. Davis,et al.  OBSERVATION OF 1000-FOLD ENHANCEMENT OF NITROGEN-15 NMR VIA PROTON-DETECTED MULTIQUANTUM COHERENCES: STUDIES OF LARGE PEPTIDES , 1985 .

[80]  L. Bonewald,et al.  Altered proteolytic cleavage of human growth hormone as a result of deamidation. , 1981, The Journal of biological chemistry.

[81]  Rudolf Rigler,et al.  Polarized fluorescence and rotational brownian motion , 1972 .

[82]  M Karplus,et al.  Active site dynamics of ribonuclease. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[83]  T. A. Jones,et al.  A graphics model building and refinement system for macromolecules , 1978 .

[84]  R. Griffey,et al.  Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR☆ , 1983 .

[85]  K. Wuethrich,et al.  The development of nuclear magnetic resonance spectroscopy as a technique for protein structure determination , 1989 .

[86]  H. Susi,et al.  Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. , 1986, Methods in enzymology.

[87]  B C Finzel,et al.  Three-dimensional structure of an antibody-antigen complex. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[88]  Ronald M. Levy,et al.  NMR relaxation parameters in molecules with internal motion: exact Langevin trajectory results compared with simplified relaxation models , 1981 .

[89]  C. Hansch,et al.  Crystal structure of avian dihydrofolate reductase containing phenyltriazine and NADPH. , 1982, The Journal of biological chemistry.

[90]  R. B. Moon,et al.  Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[91]  M. Ehrenberg,et al.  Fluorescence relaxation spectroscopy in the analysis of macromolecular structure and motion , 1976, Quarterly Reviews of Biophysics.

[92]  M Karplus,et al.  Picosecond dynamics of tyrosine side chains in proteins. , 1979, Biochemistry.

[93]  J. Hopfield,et al.  CO binding to heme proteins: A model for barrier height distributions and slow conformational changes , 1983 .

[94]  J. Anglister,et al.  Distances of tyrosine residues from a spin-label hapten in the combining site of a specific monoclonal antibody. , 1984, Biochemistry.

[95]  Kevin M. Smith,et al.  Proton nuclear magnetic resonance investigation of the conformation-dependent spin equilibrium in azide-ligated monomeric insect hemoglobins , 1983 .

[96]  C M Dobson,et al.  Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. , 1989, Biochemistry.

[97]  E. Bradbury,et al.  Thermal denaturation studies of acetylated nucleosomes and oligonucleosomes. , 1982, European journal of biochemistry.

[98]  J. Feeney,et al.  Dihydrofolate reductase. 1H resonance assignments and coenzyme-induced conformational changes. , 1986, Journal of molecular biology.

[99]  G. Fasman.  Circular dichroism analysis of chromatin and DNA--nuclear protein complexes. , 1978, Methods in cell biology.

[100]  R. Ladenstein,et al.  Electrostatic effects in a large enzyme complex: Subunit interactions and electrostatic potential field of the icosahedral β60 capsid of heavy riboflavin synthase , 1989, Proteins.

[101]  P. Artymiuk,et al.  X-ray studies of water in crystals of lysozyme. , 1983, Journal of molecular biology.

[102]  J. Blanchard,et al.  Glutathione reductase: solvent equilibrium and kinetic isotope effects. , 1988, Biochemistry.

[103]  J. Hoch,et al.  A structural study of the hydrophobic box region of lysozyme in solution using nuclear Overhauser effects. , 1980, Biochemistry.

[104]  Axel T. Brunger,et al.  A memory-efficient fast Fourier transformation algorithm for crystallographic refinement on supercomputers , 1989 .

[105]  W. Horrocks,et al.  Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems: ferricytochrome c and metmyoglobin cyanide. , 1973, Biochimica et biophysica acta.

[106]  A. Bax,et al.  Measurement of carbon-13 longitudinal relaxation using 1H detection , 1987 .

[107]  J. Kirkwood,et al.  THE NUCLEAR MAGNETIC RESONANCE SPECTRUM OF RIBONUCLEASE1 , 1957 .

[108]  M. Krahl,et al.  Diabetogenic peptide from human growth hormone: partial purification from peptic digest and long-term action in ob/ob mice. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[109]  R. Rigler,et al.  Picosecond Time Domain Spectroscopy of Structure and Dynamics in Nucleic Acids , 1986 .

[110]  A. M. Skene,et al.  TRIAL OF TISSUE PLASMINOGEN ACTIVATOR FOR MORTALITY REDUCTION IN ACUTE MYOCARDIAL INFARCTION Anglo-Scandinavian Study of Early Thrombolysis (ASSET) , 1988, The Lancet.

[111]  J. B. Johnson,et al.  Rebinding and relaxation in the myoglobin pocket. , 1987, Biophysical chemistry.

[112]  S. Fesik,et al.  Isotope-edited proton NMR study on the structure of a pepsin/inhibitor complex. , 1988, Biochemistry.

[113]  J. Bandekar,et al.  Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. , 1986, Advances in protein chemistry.

[114]  J. Andrew McCammon,et al.  The dynamic picture of protein structure , 1983 .

[115]  K Wüthrich,et al.  A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. , 1980, Biochemical and biophysical research communications.

[116]  F. Stillinger,et al.  Packing Structures and Transitions in Liquids and Solids , 1984, Science.

[117]  M. Karplus,et al.  Active site dynamics in protein molecules: A stochastic boundary molecular‐dynamics approach , 1985, Biopolymers.

[118]  M Karplus,et al.  Time dependence of atomic fluctuations in proteins: analysis of local and collective motions in bovine pancreatic trypsin inhibitor. , 1982, Biochemistry.

[119]  G. Reeke,et al.  Three-dimensional structure of beta 2-microglobulin. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[120]  Wayne A. Hendrickson,et al.  Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur , 1981, Nature.

[121]  M. Llinás,et al.  Analysis of the aromatic 1H-NMR spectrum of the kringle 5 domain from human plasminogen. Evidence for a conserved kringle fold. , 1988, European journal of biochemistry.

[122]  Lou Reinisch,et al.  Protein fluctuations, distributed coupling, and the binding of ligands to heme proteins , 1988 .

[123]  R. R. Ernst,et al.  Improvement of pulse performance in N.M.R. coherence transfer experiments , 1983 .

[124]  K. Wüthrich,et al.  15N-labeled P22 c2 repressor for nuclear magnetic resonance studies of protein-DNA interactions , 1987, European Biophysics Journal.

[125]  K. Wüthrich.  NMR of proteins and nucleic acids , 1988 .

[126]  M. Karplus,et al.  Fluorescence depolarization of tryptophan residues in proteins: a molecular dynamics study. , 1983, Biochemistry.

[127]  W. Caughey,et al.  Infrared spectroscopy of a single cell--the human erythrocyte. , 1988, Biochemical and biophysical research communications.

[128]  M. Karplus,et al.  Restraints in temperature-factor refinement for macromolecules: an evaluation by molecuar dynamics , 1985 .

[129]  H. Mantsch,et al.  New insight into protein secondary structure from resolution-enhanced infrared spectra. , 1988, Biochimica et biophysica acta.

[130]  R. Poljak,et al.  Three-dimensional structure of immunoglobulins. , 1979, Annual review of biochemistry.

[131]  L. Yu,et al.  Directly observed 15N NMR spectra of uniformly enriched proteins. , 1987, Biochemistry.

[132]  Richard R. Ernst,et al.  Investigation of exchange processes by two‐dimensional NMR spectroscopy , 1979 .

[133]  J. Richardson,et al.  The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.

[134]  A M Gronenborn,et al.  Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. , 1989, Critical reviews in biochemistry and molecular biology.

[135]  M. Karplus,et al.  Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[136]  A. Gronenborn,et al.  Long‐range 15N‐1H correlation as an aid to sequential proton resonance assignment of proteins Application to the DNA‐binding protein ner from phage Mu , 1988, FEBS letters.

[137]  J. Feeney,et al.  15N and 1H NMR evidence for multiple conformations of the complex of dihydrofolate reductase with its substrate, folate , 1987, FEBS letters.

[138]  C. Dobson,et al.  Proton nuclear Overhauser effects and protein dynamics , 1981 .

[139]  NMR OF PROTONS COUPLED TO CARBON-13 NUCLEI ONLY , 1981 .

[140]  M. Karplus,et al.  Hidden thermodynamics of mutant proteins: a molecular dynamics analysis. , 1989, Science.

[141]  R. Zinkernagel,et al.  Identical Vβ T-cell receptor genes used in alloreactive cytotoxic and antigen plus I–A specific helper T cells , 1985, Nature.

[142]  L. C. Allen,et al.  Strong, positive‐ion hydrogen bonds: The binary complexes formed from NH3, OH2, FH, PH3, SH2, and ClH , 1980 .

[143]  G. Schulz,et al.  The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates. , 1983, The Journal of biological chemistry.

[144]  B. Oh,et al.  Carbon-13-spin-system-directed strategy for assigning cross peaks in the COSY fingerprint region of a protein , 1989 .

[145]  G. Bricogne,et al.  Methods and programs for direct‐space exploitation of geometric redundancies , 1976 .

[146]  M. Karplus,et al.  Crystallographic refinement by simulated annealing: application to crambin , 1989 .

[147]  D. Wiley,et al.  Crystallization and X-ray diffraction studies on the histocompatibility antigens HLA-A2 and HLA-A28 from human cell membranes. , 1985, Journal of molecular biology.

[148]  G. L. Kenyon,et al.  Studies of macromolecular structure by 13 C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins. , 1973, Journal of the American Chemical Society.

[149]  J. Bolin,et al.  Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. , 1982, The Journal of biological chemistry.

[150]  C. Janeway,et al.  Molecular characterization of antibodies bearing Id-460. II. Molecular basis for Id-460 expression , 1985, The Journal of experimental medicine.

[151]  F. Richards,et al.  Anion binding and pH-dependent electrostatic effects in ribonuclease. , 1982, Biochemistry.

[152]  W. Caughey,et al.  Determination of anesthetic molecule environments by infrared spectroscopy. I. Effects of solvating molecule structure on nitrous oxide spectra. , 1985, Archives of biochemistry and biophysics.

[153]  D. Doddrell,et al.  Conformation and segmental motion of native and denatured ribonuclease A in solution. Application of natural-abundance carbon-13 partially relaxed Fourier transform nuclear magnetic resonance. , 1971, Journal of the American Chemical Society.

[154]  K. Wüthrich.  Protein structure determination in solution by nuclear magnetic resonance spectroscopy. , 1989, Science.

[155]  G. Lomakka,et al.  Picosecond Single Photon Fluorescence Spectroscopy of Nucleic Acids , 1984, Topical Meeting on Ultrafast Phenomena.

[156]  K. Rothschild,et al.  Fourier transform infrared techniques for probing membrane protein structure. , 1988, Annual review of biophysics and biophysical chemistry.

[157]  Wolfgang Doster,et al.  Dynamical transition of myoglobin revealed by inelastic neutron scattering , 1989, Nature.

[158]  J. H. Brown.  A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules , 1988, Nature.

[159]  T. Grundström,et al.  The role of protein surface charges in ion binding , 1988, Nature.

[160]  C. Walsh,et al.  Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide. , 1983, Biochemistry.

[161]  D. Leahy,et al.  Sequences of 12 monoclonal anti-dinitrophenyl spin-label antibodies for NMR studies. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[162]  C. Nicolini.  Biophysics and cancer , 1986 .

[163]  E. Lattman,et al.  Representation of phase probability distributions for simplified combination of independent phase information , 1970 .

[164]  A. Böck,et al.  Genes for stable RNA in the extreme thermophile Thermoproteus tenax: introns and transcription signals , 1987, The EMBO journal.

[165]  L. Nilsson,et al.  Structural fluctuations of a helical polypeptide traversing a lipid bilayer. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[166]  P. Wright,et al.  Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques. , 1987, Journal of molecular biology.

[167]  M. Levitt,et al.  Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme. , 1985, Journal of molecular biology.

[168]  J. Kirkwood.  Statistical Mechanics of Fluid Mixtures , 1935 .

[169]  J. Strominger,et al.  Human class II major histocompatibility complex genes and proteins. , 1988, Annual review of biochemistry.

[170]  K. Wüthrich,et al.  Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. , 1983, Biochemical and biophysical research communications.

[171]  S. Harrison.  Multiple modes of subunit association in the structures of simple spherical viruses , 1984 .

[172]  K Wüthrich,et al.  Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance. , 1982, Journal of molecular biology.

[173]  Wayne A. Hendrickson,et al.  A restrained-parameter thermal-factor refinement procedure , 1980 .

[174]  A. Bax,et al.  Simplification of two-dimensional NOE spectra of proteins by 13C labeling , 1987 .

[175]  B. Roth,et al.  Recent progress in the medicinal chemistry of 2,4-diaminopyrimidines. , 1982, Progress in medicinal chemistry.

[176]  Hans Frauenfelder,et al.  Temperature-dependent X-ray diffraction as a probe of protein structural dynamics , 1979, Nature.

[177]  M. Karplus,et al.  Electronic structure of cyanide complexes of hemes and heme proteins. , 1971, Journal of molecular biology.

[178]  W. Baumeister,et al.  Decoration and shadowing of freeze-etched catalase crystals. , 1985, Ultramicroscopy.

[179]  A. Drake,et al.  An analysis of the 225–230‐nm CD band of elapid toxins , 1988, Biopolymers.

[180]  W. Zinth,et al.  Femtosecond Spectroscopy of the Primary Events of Bacterial Photosynthesis , 1986 .

[181]  Måns Ehrenberg,et al.  Rotational brownian motion and fluorescence intensify fluctuations , 1974 .

[182]  M Karplus,et al.  Conformations of intermediates in the folding of the pancreatic trypsin inhibitor. , 1987, Journal of molecular biology.

[183]  R. Dwek,et al.  NMR in Biological Research: Peptides and Proteins , 1978 .

[184]  J. Anglister,et al.  Nonaromatic amino acids in the combining site region of a monoclonal anti-spin-label antibody. , 1984, Biochemistry.

[185]  L. Gráf,et al.  Human pituitary growth hormone: isolation and properties of two biologically active fragments from plasmin digests. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[186]  M. Levitt,et al.  Automatic identification of secondary structure in globular proteins. , 1977, Journal of molecular biology.

[187]  H Frauenfelder,et al.  Control and pH dependence of ligand binding to heme proteins. , 1982, Biochemistry.

[188]  P. Bolton.  Heteronuclear relay transfer spectroscopy with proton detection , 1985 .

[189]  P. A. Peterson,et al.  Chemical, physical-chemical, and immunological properties of papain-solubilized human transplatation antigens. , 1979, Biochemistry.

[190]  F. Stillinger,et al.  Improved simulation of liquid water by molecular dynamics , 1974 .

[191]  A. Bax,et al.  1H and13C Assignments from Sensitivity-Enhanced Detection of Heteronuclear Multiple-Bond Connectivity by 2D Multiple Quantum NMR , 1986 .

[192]  B. Oh,et al.  Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment. , 1988, Science.

[193]  E. Ulrich,et al.  NMR relaxation study of internal motions in Staphylococcal nuclease , 1988 .

[194]  M. Karplus,et al.  CHARMM: A program for macromolecular energy, minimization, and dynamics calculations , 1983 .

[195]  S. Fesik,et al.  Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra , 1988 .

[196]  K. Wüthrich,et al.  Carbon-13 nuclear magnetic resonance studies of the selectively isotope-labeled reactive site peptide bond of the basic pancreatic trypsin inhibitor in the complexes with trypsin, trypsinogen, and anhydrotrypsin. , 1980, Biochemistry.

[197]  H. Berendsen,et al.  ALGORITHMS FOR MACROMOLECULAR DYNAMICS AND CONSTRAINT DYNAMICS , 1977 .

[198]  G. Wagner,et al.  Measurement of 13C spin-spin relaxation times by two-dimensional heteronuclear 1H13C correlation spectroscopy , 1989 .

[199]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[200]  S. Provencher,et al.  Estimation of globular protein secondary structure from circular dichroism. , 1981, Biochemistry.

[201]  Claudio Nicolini,et al.  Pepto: An expert system for automatic peak assignment of two‐dimensional nuclear magnetic resonance spectra of proteins , 1990 .

[202]  K Wüthrich,et al.  Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. , 1982, Journal of molecular biology.

[203]  G. Clore,et al.  Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[204]  Ad Bax,et al.  Line narrowing of amide proton resonances in 2D NMR spectra of proteins , 1989 .

[205]  L. J. Lewis,et al.  The 20,000-dalton variant of human growth hormone: location of the amino acid deletions. , 1980, Biochemical and biophysical research communications.

[206]  P. Parham,et al.  Carbohydrate moiety of HLA antigens. Antigenic properties and amino acid sequences around the site of glycosylation. , 1977, The Journal of biological chemistry.

[207]  E. Knapp,et al.  Protein dynamics. Mössbauer spectroscopy on deoxymyoglobin crystals. , 1982, Journal of molecular biology.

[208]  F. Bovey,et al.  Polymer NSR spectroscopy. I. The motion and configuration of polymer chains in solution , 1959 .

[209]  M. Karplus,et al.  Structure and internal mobility of proteins: A molecular dynamics study of hen egg white lysozyme , 1986, Biopolymers.

[210]  G A Petsko,et al.  Fluctuations in protein structure from X-ray diffraction. , 1984, Annual review of biophysics and bioengineering.

[211]  H. Grey,et al.  Autologous peptides constitutively occupy the antigen binding site on Ia. , 1988, Science.

[212]  H. Crespi,et al.  Proton Magnetic Resonance of Proteins Fully Deuterated except for 1H-Leucine Side Chains , 1968, Science.

[213]  L. A. Day,et al.  Circular dichroism and ultraviolet absorption of a deoxyribonucleic acid binding protein of filamentous bacteriophage. , 1973, Biochemistry.

[214]  Optimising selective deuteration of proteins for 2D 1H NMR detection and assignment studies Application to the Phe residues of Lactobacillus casei dihydrofolate reductase , 1989 .

[215]  D. Lancet,et al.  Heavy chain of HLA-A and HLA-B antigens is conformationally labile: a possible role for beta 2-microglobulin. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[216]  George M. Church,et al.  A structure-factor least-squares refinement procedure for macromolecular structures using constrained and restrained parameters , 1977 .

[217]  D. Cowburn,et al.  Assignment of 15N NMR signals in bovine pancreatic trypsin inhibitor , 1987 .

[218]  J. Strominger,et al.  Purification and characterization of class II histocompatibility antigens from a homozygous human B cell line. , 1987, The Journal of biological chemistry.

[219]  A. Bax,et al.  Long range heteronuclear correlation. A powerful tool for the NMR analysis of medium-size proteins , 1988 .

[220]  G. McFeters,et al.  Induction and Characterization of β-Galactosidase in an Extreme Thermophile , 1972, Journal of bacteriology.

[221]  A. Bacher.  Heavy riboflavin synthase from Bacillus subtilis. , 1986, Methods in enzymology.

[222]  P. Seeburg,et al.  Efficient bacterial expression of bovine and porcine growth hormones. , 1983, DNA.

[223]  Robert L. Baldwin,et al.  NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A , 1988, Nature.

[224]  D. Thouless,et al.  Models of Disorder: The Theoretical Physics of Homogeneously Disordered Systems , 1979 .

[225]  R. Kretsinger,et al.  Structure and evolution of calcium-modulated proteins. , 1980, CRC critical reviews in biochemistry.

[226]  R. Boelens,et al.  Three-dimensional J-resolved NMR spectroscopy , 1987 .

[227]  A. Bax,et al.  NMR signal assignments of amide protons in the alpha-helical domains of staphylococcal nuclease. , 1988, Biochemistry.

[228]  J. Markley,et al.  Two-dimensional nuclear magnetic resonance spectroscopy of proteins: an overview. , 1989, Methods in enzymology.

[229]  S. Hyberts,et al.  Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c. , 1987, European journal of biochemistry.

[230]  G. K. Ackers,et al.  Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[231]  E. Kabat,et al.  Sequences of proteins of immunological interest , 1991 .

[232]  W. Zillig,et al.  Transcription termination in the archaebacterium Sulfolobus: signal structures and linkage to transcription initiation. , 1988, Nucleic acids research.

[233]  M. Levitt,et al.  Contribution of tryptophan residues to the combining site of a monoclonal anti dinitrophenyl spin-label antibody. , 1987, Biochemistry.

[234]  L. Kay,et al.  Sensitivity enhancement of 13C T1 measurements via polarization transfer , 1987 .

[235]  M. J. Chatfield,et al.  Solvent isotope effects on NMR spectral parameters in high-spin ferric hemoproteins: an indirect probe for distal hydrogen bonding. , 1988, Biochimica et biophysica acta.

[236]  J. M. Kwiatkoski,et al.  FT-IR microspectrometry advances , 1987, Nature.

[237]  G. Careri,et al.  Soliton-assisted unidirectional circulation in a biochemical cycle. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[238]  W. F. van Gunsteren,et al.  Effect of constraints on the dynamics of macromolecules , 1982 .

[239]  S. Forsén,et al.  Chapter 4 – Biophysical Studies of Calmodulin , 1986 .

[240]  James E. Roberts,et al.  Two-dimensional heteronuclear chemical shift correlation spectroscopy in rotating solids , 1984 .

[241]  M. Druger,et al.  EVOLUTIONARY DIVERGENCE BETWEEN TWO POPULATIONS OF DROSOPHILA PSEUDOOBSCURA , 1977, Evolution; international journal of organic evolution.

[242]  D. G. Davis,et al.  Paramagnetic proton nuclear magnetic resonance shifts of metmyoglobin, methemoglobin, and hemin derivatives. , 1968, Journal of the American Chemical Society.

[243]  J. Anglister,et al.  Magnetic resonance of a monoclonal anti-spin-label antibody , 1984 .

[244]  J. Markley,et al.  Methods of Stable-Isotope-Assisted Protein NMR Spectroscopy in Solution , 1989 .

[245]  M. Kainosho,et al.  Assignment of the three methionyl carbonyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution. , 1982, Biochemistry.

[246]  M Karplus,et al.  Dynamics of proteins: elements and function. , 1983, Annual review of biochemistry.

[247]  R. Perham,et al.  An amino acid sequence in the active site of lipoamide dehydrogenase from pig heart. , 1974, Biochemical Journal.

[248]  Ronald M. Levy,et al.  Vibrational approach to the dynamics of an α‐helix , 1979 .

[249]  A. Bacher,et al.  Biosynthesis of riboflavin in Bacillus subtilis: function and genetic control of the riboflavin synthase complex , 1978, Journal of bacteriology.

[250]  M. Karplus,et al.  Internal motion of proteins: nuclear magnetic resonance measurements and dynamic simulations. , 1986, Methods in enzymology.

[251]  B. Sykes,et al.  Backbone dynamics of a model membrane protein: 13C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein. , 1986, Biochemistry.

[252]  R. Levy,et al.  Interactions of antibody aromatic residues with a peptide of cholera toxin observed by two-dimensional transferred nuclear Overhauser effect difference spectroscopy. , 1989, Biochemistry.

[253]  H. Bunn,et al.  Hemoglobin: Molecular, Genetic and Clinical Aspects , 1984 .

[254]  Jen-Tsi Yang,et al.  Two-Point Calibration of Circular Dichrometer with d-10-Camphorsulfonic Acid , 1977 .

[255]  S. Ogawa,et al.  Assignments of the paramagnetically shifted heme methyl nuclear magnetic resonance peaks of cyanometmyoglobin by selective deuteration. , 1974, Journal of molecular biology.

[256]  Kurt Wüthrich,et al.  Experimental techniques of two-dimensional correlated spectroscopy , 1980 .

[257]  N. Brown,et al.  Nucleotide sequence of a gene from the Pseudomonas transposon Tn501 encoding mercuric reductase. , 1983, Biochemistry.

[258]  M. Summers.  113Cd NMR spectroscopy of coordination compounds and proteins , 1988 .

[259]  P. Marrack,et al.  The antigen-specific, major histocompatibility complex-restricted receptor on T cells. , 1986, Advances in immunology.

[260]  S. Phillips,et al.  Structure and refinement of oxymyoglobin at 1.6 A resolution. , 1980, Journal of molecular biology.

[261]  J. Markley,et al.  Staphylococcal nuclease active-site amino acids: pH dependence of tyrosines and arginines by 13C NMR and correlation with kinetic studies. , 1989, Biochemistry.

[262]  P. Lu,et al.  Lambda cro repressor complex with OR3 DNA: 15N NMR observations. , 1987, Biochemistry.

[263]  H. Senn,et al.  Protein structure and interactions by combined use of sequential NMR assignments and isotope labeling , 1987 .

[264]  L. Kay,et al.  Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. , 1989, Biochemistry.

[265]  R D Young,et al.  Protein states and proteinquakes. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[266]  G. Montelione,et al.  2D chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation , 1989 .

[267]  M. A. Saper,et al.  The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens , 1987, Nature.

[268]  Side chain mobility in bovine calbindin D9k. Rotational motion of Tyr13. , 1990, European journal of biochemistry.

[269]  G. Bodenhausen,et al.  Principles of nuclear magnetic resonance in one and two dimensions , 1987 .

[270]  M. Perutz,et al.  Molecular Pathology of Human Haemoglobin: Stereochemical Interpretation of Abnormal Oxygen Affinities , 1971, Nature.

[271]  A. Fairlamb,et al.  Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. , 1986, Biochemistry.

[272]  M. Brunori,et al.  Enzyme Proteins. (Book Reviews: Hemoglobin and Myoglobin in Their Reactions with Ligands) , 1971 .

[273]  F. Richards,et al.  NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. , 1988, Biochemistry.

[274]  S. Forsén,et al.  43Ca NMR studies of calcium binding to proteins: Interpretation of experimental data by bandshape analysis , 1983 .

[275]  J. Feeney,et al.  The charge state of trimethoprim bound to Lactobacillus casei dihydrofolate reductase , 1981, FEBS letters.

[276]  A. Lesk,et al.  How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. , 1980, Journal of molecular biology.

[277]  Barry Robson,et al.  Introduction to proteins and protein engineering , 1986 .

[278]  I. Kuntz,et al.  Diffusion‐collision model for the folding kinetics of myoglobin , 1988, Proteins.

[279]  H Frauenfelder,et al.  Dynamics of ligand binding to myoglobin. , 1975, Biochemistry.

[280]  D. Isenman,et al.  The structure and function of immunoglobulin domains: studies with beta-2-microglobulin on the role of the intrachain disulfide bond. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[281]  J. Satterlee,et al.  Axial histidyl imidazole non-exchangeable proton resonances as indicators of imidazole hydrogen bonding in ferric cyanide complexes of heme peroxidases. , 1982, Biochimica et biophysica acta.

[282]  S. Fesik,et al.  Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a. , 1989, Biochemistry.

[283]  D. G. Davis,et al.  Natural-abundance 15N NMR studies of Turkey ovomucoid third domain. Assignment of peptide 15N resonances to the residues at the reactive site region via proton-detected multiple-quantum coherence , 1986 .

[284]  J. Markley,et al.  Assignment of the histidine proton magnetic resonance peaks of soybean trypsin inhibitor (Kunitz) by a differertial deuterium exchange technique. , 1975, Biochemistry.

[285]  A. Fairlamb,et al.  Trypanothione reductase from Trypanosoma cruzi. Purification and characterization of the crystalline enzyme. , 1987, European Journal of Biochemistry.

[286]  F. A. Cotton,et al.  Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[287]  C. Chothia,et al.  Hydrophobic bonding and accessible surface area in proteins , 1974, Nature.

[288]  W. M. Westler,et al.  Two-dimensional NMR strategies for carbon-carbon correlations and sequence-specific assignments in carbon-13 labeled proteins , 1988 .

[289]  J. Feeney,et al.  Dynamics of trimethoprim bound to dihydrofolate reductase. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[290]  A. Malcolm.  Amino acid sequence homology. , 1979, Journal of theoretical biology.

[291]  Champion,et al.  Spectral broadening in biomolecules. , 1986, Physical review letters.

[292]  L. Franco,et al.  Structural studies on histones H1. Circular dichroism and difference spectroscopy of the histones H1 and their trypsin-resistant cores from calf thymus and from the fruit fly Ceratitis capitata. , 1980, Biochemistry.

[293]  J. Feeney,et al.  Direct 19F NMR observation of the conformational selection of optically active rotamers of the antifolate compound fluoronitropyrimethamine bound to the enzyme dihydrofolate reductase , 1988, FEBS letters.

[294]  M. Bokranz,et al.  Nucleotide sequence of the methyl coenzyme M reductase gene cluster from Methanosarcina barkeri. , 1987, Nucleic acids research.

[295]  L. J. Perry,et al.  Unpaired cysteine-54 interferes with the ability of an engineered disulfide to stabilize T4 lysozyme. , 1986, Biochemistry.

[296]  R. R. Ernst,et al.  Novel three-dimensional NMR techniques for studies of peptides and biological macromolecules , 1987 .

[297]  K. Wüthrich,et al.  Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. , 1982, Journal of molecular biology.

[298]  P. Chambon,et al.  The segmented paper method: DNA synthesis and mutagenesis by rapid microscale "shotgun gene synthesis". , 1987, Methods in enzymology.

[299]  P. Kraulis,et al.  Three-dimensional NMR spectroscopy of a protein in solution , 1988, Nature.

[300]  B. E. Kimmel,et al.  Trypanothione reductase of Trypanosoma congolense: gene isolation, primary sequence determination, and comparison to glutathione reductase. , 1988, Biochemistry.

[301]  N. Green,et al.  Optical rotatory dispersion, circular dichroism and far-ultraviolet spectra of avidin and streptavidin. , 1966, The Biochemical journal.

[302]  S. Radford,et al.  2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning and halfway there. , 1987, Biochemical Society symposium.

[303]  M Karplus,et al.  The internal dynamics of globular proteins. , 1981, CRC critical reviews in biochemistry.

[304]  G. Wagner,et al.  Selective excitation of 1H resonances coupled to 13C. Hetero COSY and RELAY experiments with 1H detection for a protein , 1986 .

[305]  S. Opella,et al.  Protein backbone dynamics by solid-state and solution 15N NMR spectroscopy , 1987 .

[306]  R. Perham,et al.  Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. , 1986, Biochemistry.

[307]  K. Wüthrich,et al.  Editing of 2D 1H NMR spectra using X half-filters. combined use with residue-selective 15N labeling of proteins , 1986 .

[308]  W. C. Johnson,et al.  Secondary structure of proteins through circular dichroism spectroscopy. , 1988, Annual review of biophysics and biophysical chemistry.

[309]  J. Markley.  Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignments. , 1975, Biochemistry.

[310]  Y H Chen,et al.  Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. , 1974, Biochemistry.

[311]  D. Bogenhagen,et al.  Clusters of point mutations are found exclusively around rearranged antibody variable genes. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[312]  L. Pauling,et al.  The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. , 1951, Proceedings of the National Academy of Sciences of the United States of America.

[313]  N. Scrutton,et al.  Switching kinetic mechanism and putative proton donor by directed mutagenesis of glutathione reductase. , 1989, Biochemistry.

[314]  J Deisenhofer,et al.  Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 A and 1.0 A resolution. , 1980, Journal of molecular biology.

[315]  G. Montelione,et al.  Accurate measurements of homonuclear HN-H.alpha. coupling constants in polypeptides using heteronuclear 2D NMR experiments , 1989 .

[316]  C. Nicolini.  Chromatin structure: from nuclei to genes (review). , 1983, Anticancer research.

[317]  M. Karplus,et al.  Nuclear Magnetic Resonance Determination of the Angle Ψ in Peptides , 1972 .

[318]  J. Tanner.  Human Growth , 1876, Nature.

[319]  H. Scheraga,et al.  Structural Studies of Ribonuclease. XXIV. The Application of Nuclear Magnetic Resonance Spectroscopy to Distinguish between the Histidine Residues of Ribonuclease1 , 1966 .

[320]  S. Baldwin,et al.  Fourier transform infrared spectroscopic study of the structure and conformational changes of the human erythrocyte glucose transporter. , 1987, The Journal of biological chemistry.

[321]  J. Katz,et al.  Deuterated organisms: cultivation and uses. , 1966, Science.

[322]  T. A. Osipova,et al.  The effect of synthetic fragment 31-44 of human growth hormone on glucose uptake by isolated adipose tissue. , 1983, Biochemical and biophysical research communications.