Relationship between nuclear magnetic resonance chemical shift and protein secondary structure.
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[1] Kurt Wüthrich,et al. Determination of the Three-dimensional Structure of the Antennapedia Homeodomain from Drosophila in Solution by 1H Nuclear Magnetic Resonance Spectroscopy , 1993 .
[2] A. Pastore,et al. The relationship between chemical shift and secondary structure in proteins , 1990 .
[3] R. Timkovich. 15N NMR spectroscopy of Pseudomonas cytochrome c-551. , 1990, Biochemistry.
[4] G. Wider,et al. Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B. , 1990, Biochemistry.
[5] C. Dobson,et al. 1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme. , 1990, Biochemistry.
[6] F. Dahlquist,et al. Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme. , 1990, Biochemistry.
[7] Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor. , 1990, Biochemistry.
[8] Gottfried Otting,et al. Determination of the three-dimensional structure of theAntennapedia homeodomain fromDrosophila in solution by1H nuclear magnetic resonance spectroscopy , 1990 .
[9] W. Chazin,et al. 1H NMR resonance assignments, secondary structure, and global fold of Apo bovine calbindin D9k. , 1990, Biochemistry.
[10] M. Cai,et al. NMR comparison of prokaryotic and eukaryotic cytochromes c. , 1990, Biochemistry.
[11] V. Saudek,et al. Sequence-specific 1H NMR assignment and secondary structure of neuropeptide Y in aqueous solution. , 1990, Biochemistry.
[12] L. Kay,et al. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. , 1990, Biochemistry.
[13] L. Kay,et al. A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin , 1990 .
[14] B. Oh,et al. Multinuclear magnetic resonance studies of the 2Fe.cntdot.2S* ferredoxin from Anabaena species strain PCC 7120. 1. Sequence-specific hydrogen-1 resonance assignments and secondary structure in solution of the oxidized form , 1990 .
[15] A. Gronenborn,et al. Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy. , 1990, Biochemistry.
[16] R. J. Williams,et al. Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry. , 1990, Journal of molecular biology.
[17] R. M. Justice,et al. Complete sequence-specific 1H NMR assignments for human insulin. , 1990, Biochemistry.
[18] P. S. Kim,et al. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. , 1990, Biochemistry.
[19] M. Caffrey,et al. Assignment of the 1H and 15N NMR spectra of Rhodobacter capsulatus ferrocytochrome c2. , 1990, Biochemistry.
[20] D. Cowburn,et al. Nitrogen-15 chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin [Erratum to document cited in CA111(17):149076x] , 1990 .
[21] S. Hyberts,et al. Sequence-specific 1H NMR assignments and secondary structure of eglin c. , 1990, Biochemistry.
[22] L. Kay,et al. Studies on the solution conformation of human thioredoxin using heteronuclear 15N-1H nuclear magnetic resonance spectroscopy. , 1990, Biochemistry.
[23] I. Kuntz,et al. Structural studies of cytochrome b5: complete sequence-specific resonance assignments for the trypsin-solubilized microsomal ferrocytochrome b5 obtained from pig and calf. , 1990, Biochemistry.
[24] A. Bacher,et al. A two-dimensional 1H NMR study on Megasphaera elsdenii flavodoxin in the reduced state. Sequential assignments. , 1990, European journal of biochemistry.
[25] R. Norton,et al. Sequential 1H-NMR assignments and secondary structure of the sea anemone polypeptide anthopleurin-A. , 1990, European journal of biochemistry.
[26] M. Summers,et al. High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach. , 1990, Biochemistry.
[27] J. Markley,et al. Two-dimensional NMR studies of staphylococcal nuclease. 1. Sequence-specific assignments of hydrogen-1 signals and solution structure of the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+ ternary complex. , 1990, Biochemistry.
[28] A. Gronenborn,et al. Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinase inhibitors. , 1990, Biochemistry.
[29] R. Kaptein,et al. Sequence-specific 1H NMR assignment and secondary structure of the Arc repressor of bacteriophage P22, as determined by two-dimensional 1H NMR spectroscopy. , 1989, Biochemistry.
[30] A M Gronenborn,et al. Determination of the secondary structure of interleukin-8 by nuclear magnetic resonance spectroscopy. , 1989, The Journal of biological chemistry.
[31] P. Kraulis,et al. Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. , 1989, Biochemistry.
[32] D. Cowburn,et al. 15N Chemical Shifts of Backbone Amides in Bovine Pancreatic Trypsin Inhibitor and Apamin , 1989 .
[33] H. Dyson,et al. Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold. , 1989, Biochemistry.
[34] F. Richards,et al. A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin. , 1989, Biochemistry.
[35] H. Scheraga,et al. Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution. , 1989, Biochemistry.
[36] W. Chazin,et al. 1H NMR studies of porcine calbindin D9k in solution: sequential resonance assignment, secondary structure, and global fold. , 1989, Biochemistry.
[37] O. Jardetzky,et al. α-Proton chemical shifts and secondary structure in proteins , 1989 .
[38] A. Bax,et al. Staphylococcal nuclease: sequential assignments and solution structure. , 1989, Biochemistry.
[39] 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.
[40] D. Fry,et al. Solution structure of an analogue of vasoactive intestinal peptide as determined by two-dimensional NMR and circular dichroism spectroscopies and constrained molecular dynamics. , 1989, Biochemistry.
[41] L. Chiche,et al. 1H 2D NMR and distance geometry study of the folding of Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family. , 1989, Biochemistry.
[42] G. Clore,et al. A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure. , 1989, Biochemistry.
[43] R. Powers,et al. Solution conformation of a synthetic fragment of human pituitary growth hormone. Two-dimensional NMR of an alpha-helical dimer. , 1989, Biochemistry.
[44] S. Brown,et al. 1H NMR assignment and secondary structural elements of human transforming growth factor alpha. , 1989, Biochemistry.
[45] A. Wand,et al. Proton resonance assignments of horse ferricytochrome c. , 1989, Biochemistry.
[46] R. J. Williams,et al. Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy. , 1989, Journal of molecular biology.
[47] J. Markley,et al. Two-dimensional nuclear magnetic resonance spectroscopy of proteins: an overview. , 1989, Methods in enzymology.
[48] P. Wright,et al. 1H NMR studies of human C3a anaphylatoxin in solution: sequential resonance assignments, secondary structure, and global fold. , 1988, Biochemistry.
[49] A. Padilla,et al. Two-dimensional 1H nuclear magnetic resonance study of pike pI 5.0 parvalbumin (Esox lucius). Sequential resonance assignments and folding of the polypeptide chain. , 1988, Journal of molecular biology.
[50] E. Tüchsen,et al. Carbonyl 13C NMR spectrum of basic pancreatic trypsin inhibitor: resonance assignments by selective amide hydrogen isotope labeling and detection of isotope effects on 13C nuclear shielding. , 1988, Biochemistry.
[51] K. Wüthrich,et al. Secondary structure determination for alpha-neurotoxin from Dendroaspis polylepis polylepis based on sequence-specific 1H-nuclear-magnetic-resonance assignments. , 1988, European journal of biochemistry.
[52] I. Brand,et al. Properties of a 19-kDa Zn2+-binding protein and sequence of the Zn2+-binding domains. , 1988, European journal of biochemistry.
[53] P. Wright,et al. 1H NMR studies of plastocyanin from Scenedesmus obliquus: complete sequence-specific assignment, secondary structure analysis, and global fold. , 1988, Biochemistry.
[54] P. Kraulis,et al. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. , 1988, Biochemistry.
[55] J. Richardson,et al. Amino acid preferences for specific locations at the ends of alpha helices. , 1988, Science.
[56] P. Gooley,et al. Location of an alpha-helix in fragment 96-133 from bovine somatotropin by 1H NMR spectroscopy. , 1988, Biochemistry.
[57] E. Zuiderweg,et al. Sequence-specific assignments in the 1H NMR spectrum of the human inflammatory protein C5a. , 1988, Biochemistry.
[58] I. Kuntz,et al. Structural studies of alpha-bungarotoxin. 1. Sequence-specific 1H NMR resonance assignments. , 1988, Biochemistry.
[59] A. D. Robertson,et al. Two-dimensional NMR studies of Kazal proteinase inhibitors. 1. Sequence-specific assignments and secondary structure of turkey ovomucoid third domain. , 1988, Biochemistry.
[60] H. Scheraga,et al. Sequence-specific 1H NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth factor. , 1988, Biochemistry.
[61] C. Dobson,et al. Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. , 1988, Biochemistry.
[62] F. Richards,et al. NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. , 1988, Biochemistry.
[63] A. Mildvan,et al. Solution structure of the 45-residue MgATP-binding peptide of adenylate kinase as examined by 2-D NMR, FTIR, and CD spectroscopy. , 1986, Biochemistry.
[64] Hans Robert Kalbitzer,et al. Distribution of chemical shifts in 1H nuclear magnetic resonance spectra of proteins , 1988 .
[65] K. Wüthrich,et al. The secondary structure of the toxin ATX Ia from Anemonia sulcata in aqueous solution determined on the basis of complete sequence-specific 1H-NMR assignments. , 1988, European Journal of Biochemistry.
[66] P. Driscoll,et al. 1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin. , 1987, European journal of biochemistry.
[67] A. Gronenborn,et al. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. , 1987, Biochemistry.
[68] K. Wüthrich,et al. Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica. , 1987, European journal of biochemistry.
[69] A. Pardi,et al. Two-dimensional NMR studies of the antimicrobial peptide NP-5. , 1987, Biochemistry.
[70] G M Clore,et al. Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structure. , 1987, Journal of molecular biology.
[71] A. Preuss,et al. Proton Nuclear Magnetic Resonance Study of Hirudin: Resonance Assignment and Secondary Structure? , 1987 .
[72] K Wüthrich,et al. Complete sequence-specific 1H nuclear magnetic resonance assignments for the alpha-amylase polypeptide inhibitor tendamistat from Streptomyces tendae. , 1986, Journal of molecular biology.
[73] C. W. Hilbers,et al. Sequential resonance assignments as a basis for the determination of a three-dimensional structure of protein E-L30 of Escherichia coli. , 1986, Journal of molecular biology.
[74] G. Drobny,et al. Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 1. Sequential resonance assignments. , 1986, Biochemistry.
[75] D E Wemmer,et al. NMR analysis and sequence of toxin II from the sea anemone Radianthus paumotensis. , 1986, Biochemistry.
[76] G. Wagner,et al. Toward the complete assignment of the carbon nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor. , 1986, Biochemistry.
[77] A. Gronenborn,et al. Solution structure of human growth hormone releasing factor. Combined use of circular dichroism and nuclear magnetic resonance spectroscopy. , 1986, Journal of molecular biology.
[78] J H Prestegard,et al. Secondary structure of acyl carrier protein as derived from two-dimensional 1H NMR spectroscopy. , 1986, Biochemistry.
[79] M. Williamson,et al. 1H-NMR assignment and secondary structure of a herpes simplex virus glycoprotein D-1 antigenic domain. , 1986, European journal of biochemistry.
[80] K. Wüthrich,et al. Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2. , 1986, European journal of biochemistry.
[81] D. Wemmer,et al. Proton NMR studies of .lambda. cro repressor. 2. Sequential resonance assignments of the proton NMR spectrum , 1985 .
[82] Wim G. J. Hol,et al. The role of the α-helix dipole in protein function and structure , 1985 .
[83] I. Ando,et al. Conformational characterization of solid polypeptides by carbon-13 NMR recorded by the cross polarization-magic angle spinning method: conformation-dependent carbon-13 chemical shifts of oligo- and poly(γ-benzyl L-glutamates) and sequential copolymers of γ-benzyl and γ-methyl L-glutamates and qualit , 1984 .
[84] E. Baker,et al. Hydrogen bonding in globular proteins. , 1984, Progress in biophysics and molecular biology.
[85] K. Wüthrich,et al. Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy. , 1983, European journal of biochemistry.
[86] K. Wüthrich,et al. Protein conformation and proton nuclear-magnetic-resonance chemical shifts. , 1983, European journal of biochemistry.
[87] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[88] H. Kricheldorf,et al. Secondary structure of peptides. 3. Carbon-13 NMR cross polarization/magic angle spinning spectroscopic characterization of solid polypeptides , 1983 .
[89] G. Wider,et al. Assignment of the 1H nuclear magnetic resonance spectrum of the proteinase inhibitor IIA from bull seminal plasma by two-dimensional nuclear magnetic resonance at 500 MHz. , 1983, Journal of molecular biology.
[90] Robert J.P. Williams,et al. Structural information from NMR secondary chemical shifts of peptide α C−H protons in proteins , 1983 .
[91] D. Wemmer,et al. Structure of apamin in solution: a two-dimensional nuclear magnetic resonance study. , 1983, Biochemistry.
[92] K. Wüthrich,et al. Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor homologue K from Dendroaspis polylepis polylepis. Two-dimensional nuclear magnetic resonance at 360 and 500 MHz. , 1982, Journal of molecular biology.
[93] N. Clayden,et al. Peptide group shifts , 1982 .
[94] K Wüthrich,et al. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor. , 1982, Journal of molecular biology.
[95] K. Wüthrich,et al. Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor. , 1979, Biochimica et biophysica acta.
[96] 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 .
[97] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[98] R. Ditchfield. Theoretical studies of magnetic shielding in H2O and (H2O)2 , 1976 .
[99] Tigelaar Hl,et al. Molecular Zeeman effect in formamide and the -proton chemical shift in poly(L-alanine). , 1972 .
[100] W. G. Craig,et al. NMR—the chemical shift—IV: The anisotropies of the carbonyl group , 1970 .
[101] G. N. Ramachandran,et al. Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.
[102] D. Wilson,et al. Magnetic resonance studies of macromolecules. I. Aromatic-methyl interactions and helical structure effects in lysozyme. , 1967, Biochemistry.
[103] D. Meadows,et al. Nuclear magnetic resonance studies of helix-coil transitions in polyamino acids. , 1967, Journal of molecular biology.
[104] Martin Karplus,et al. Vicinal Proton Coupling in Nuclear Magnetic Resonance , 1963 .
[105] Kritskiĭ Ga,et al. [AUTOLYSIS OF BONE MARROW NUCLEIC ACIDS UNDER NORMAL CONDITIONS AND AFTER X-IRRADIATION]. , 1963 .
[106] D. Bonner. [Enzyme formation and the genetic code]. , 1963, Biokhimiia.