The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure

[1]  P. Gooley,et al.  Location of an alpha-helix in fragment 96-133 from bovine somatotropin by 1H NMR spectroscopy. , 1988, Biochemistry.

[2]  P K Warme,et al.  Computation of structures of homologous proteins. Alpha-lactalbumin from lysozyme. , 1974, Biochemistry.

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

[4]  A. Wada,et al.  ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains , 1983, FEBS letters.

[5]  O. Ptitsyn,et al.  Physical nature of the phase transition in globular proteins , 1986, FEBS letters.

[6]  D A Yphantis,et al.  Acid unfolding and self-association of recombinant Escherichia coli derived human interferon gamma. , 1987, Biochemistry.

[7]  H. Kim,et al.  Fusion of phospholipid vesicles induced by alpha-lactalbumin at acidic pH. , 1986, Biochemistry.

[8]  C. Vita,et al.  Folding of thermolysin fragments. Identification of the minimum size of a carboxyl-terminal fragment that can fold into a stable native-like structure. , 1985, Journal of molecular biology.

[9]  R. L. Baldwin,et al.  Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[10]  K. Kuwajima,et al.  Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin. , 1989, Journal of molecular biology.

[11]  O. Ptitsyn,et al.  The ‘molten globule’ state is involved in the translocation of proteins across membranes? , 1988, FEBS letters.

[12]  T. Creighton,et al.  Single amino acid mutations block a late step in the folding of beta-lactamase from Staphylococcus aureus. , 1985, Journal of molecular biology.

[13]  H. Levine,et al.  Structural features of human leukocyte interferon A as determined by circular dichroism spectroscopy. , 2009, International journal of peptide and protein research.

[14]  B. Nall,et al.  Guanidine hydrochloride induced unfolding of yeast iso-2 cytochrome c. , 1981, Biochemistry.

[15]  K. Yutani,et al.  pH dependence of stability of the wild-type tryptophan synthase α-subunit and two mutant proteins (Glu49 → Met or Gln) , 1980 .

[16]  T. Creighton,et al.  Energetics of protein structure and folding , 1985, Biopolymers.

[17]  K. Kuwajima,et al.  Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozyme. , 1986, Biochemistry.

[18]  D. Wetlaufer.  Nucleation, rapid folding, and globular intrachain regions in proteins. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[19]  Robert L. Baldwin,et al.  Tests of the helix dipole model for stabilization of α-helices , 1987, Nature.

[20]  B. Robson,et al.  The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformation. , 1976, The Biochemical journal.

[21]  P. Luisi,et al.  Folding of protein fragments: Conformational and biological studies on thioredoxin and its fragments , 1983, Biopolymers.

[22]  K. Kuwajima.  A folding model of α-lactalbumin deduced from the three-state denaturation mechanism , 1977 .

[23]  K. Kuwajima,et al.  Influence of Ca2+ binding on the structure and stability of bovine alpha-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra. , 2009, International journal of peptide and protein research.

[24]  E. W. Kauffman,et al.  Reversible self-association of bovine growth hormone during equilibrium unfolding. , 1986, Biochemistry.

[25]  P. S. Kim.  Amide proton exchange as a probe of protein folding pathways. , 1986, Methods in enzymology.

[26]  D. Puett,et al.  Growth hormone conformation and conformational equilibria. , 1974, Biochemistry.

[27]  M. Karplus,et al.  Protein-folding dynamics , 1976, Nature.

[28]  R. Freedman,et al.  Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes , 1988, Nature.

[29]  D. Balasubramanian,et al.  The molten globular intermediate form in the folding pathway of human carbonic anhydrase B , 1985, FEBS letters.

[30]  M. Sundaralingam,et al.  Crystallographic analysis of the three-dimensional structure of baboon alpha-lactalbumin at low resolution. Homology with lysozyme. , 1987, The Biochemical journal.

[31]  C. Vita,et al.  Domain characteristics of the carboxyl‐terminal fragment 206–316 of thermolysin: pH and ionic strength dependence of conformation , 1985 .

[32]  R. L. Baldwin,et al.  Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. , 1989, Biochemistry.

[33]  K. Kuwajima,et al.  Application of the pH-jump method to the titration of tyrosine residues in bovine alpha-lactalbumin. , 1979, Biochemistry.

[34]  O. Ptitsyn,et al.  Comparison of intramolecular packing of a protein in native and ‘molten globule’ states , 1986 .

[35]  R. Jaenicke,et al.  Folding and association of proteins. , 1982, Biophysics of structure and mechanism.

[36]  D. Goldenberg.  Genetic studies of protein stability and mechanisms of folding. , 1988, Annual review of biophysics and biophysical chemistry.

[37]  P. S. Kim,et al.  Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. , 1982, Annual review of biochemistry.

[38]  P. Privalov,et al.  Stability of protein structure and hydrophobic interaction. , 1988, Advances in protein chemistry.

[39]  C. Pace.  Determination and analysis of urea and guanidine hydrochloride denaturation curves. , 1986, Methods in enzymology.

[40]  O. Ptitsyn,et al.  An early intermediate of refolding α‐lactalbumin forms within 20 ms , 1987 .

[41]  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.

[42]  L. Regan,et al.  Characterization of a helical protein designed from first principles. , 1988, Science.

[43]  O. Ptitsyn,et al.  Sequential mechanism of refolding of carbonic anhydrase B , 1987, FEBS letters.

[44]  K. Kuwajima,et al.  Intramolecular perturbation of tryptophans induced by the protonation of ionizable groups in goat alpha-lactalbumin. , 1980, Biochimica et biophysica acta.

[45]  M. Kronman,et al.  Binding of naphthalene dyes to the N and A conformers of bovine α-lactalbumin , 1982 .

[46]  R. Kelley,et al.  Effects of guanidine hydrochloride on the refolding kinetics of denatured thioredoxin. , 1986, Biochemistry.

[47]  M. Kronman,et al.  Inter- and intramolecular interactions of -lactalbumin. XI. Comparison of the "exposure" of tyrosyl, tryptophyl, and lysyl side chains in the goat and bovine proteins. , 1972, Biochimica et biophysica acta.

[48]  O. Ptitsyn,et al.  A model of myoglobin self-organization. , 1975, Biophysical chemistry.

[49]  O. Ptitsyn,et al.  ‘Molten‐globule“ state accumulates in carbonic anhydrase folding , 1984, FEBS letters.

[50]  K. Kuwajima,et al.  Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin. , 1985, Biochemistry.

[51]  K. Kuwajima,et al.  Three-state denaturation of α-lactalbumin by guanidine hydrochloride , 1976 .

[52]  J. Schellman.  The thermodynamic stability of proteins. , 1987, Annual review of biophysics and biophysical chemistry.

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

[54]  A. Pande,et al.  Urea denaturation of horse heart ferricytochrome c. Equilibrium studies and characterization of intermediate forms. , 1980, Biochemistry.

[55]  W. Herreman,et al.  Interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles. I. A microcalorimetric and fluorescence study. , 1980, Biochimica et biophysica acta.

[56]  H. Scheraga,et al.  Folding of ribonuclease A from a partially disordered conformation: kinetic study under transition conditions , 1982 .

[57]  D. I. Stuart,et al.  α-Lactalbumin possesses a novel calcium binding loop , 1986, Nature.

[58]  D. Shortle,et al.  Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions. , 1989, Biochemistry.

[59]  K. Dill.  Theory for the folding and stability of globular proteins. , 1985, Biochemistry.

[60]  P E Wright,et al.  Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. , 1988, Biochemistry.

[61]  H. Burger,et al.  The properties of bovine growth hormone. I. Behavior in acid solution. , 1966, The Journal of biological chemistry.

[62]  A. Fink,et al.  Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. , 1989, Biochemistry.

[63]  M. Jiménez,et al.  1H-NMR assignment and folding of the isolated ribonuclease 21-42 fragment. , 1988, European journal of biochemistry.

[64]  S Sugai,et al.  Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism , 1987, FEBS letters.

[65]  E. Padlan,et al.  Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. , 1988, The Journal of biological chemistry.

[66]  D. Brems,et al.  Folding of bovine growth hormone is consistent with the molten globule hypothesis , 1989, Proteins.

[67]  P. Privalov,et al.  Thermodynamic study of the apomyoglobin structure. , 1988, Journal of molecular biology.

[68]  P. S. Kim,et al.  Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange. , 1980, Biochemistry.

[69]  Matthews Cr,et al.  Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process. , 1981 .

[70]  A M Lesk,et al.  Folding units in globular proteins. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[71]  K. Kuwajima,et al.  Hydrogen exchange of the tryptophan residues in bovine α‐lactalbumin studied by uv spectroscopy , 1988 .

[72]  W. Pfeil.  Is thermally denatured protein unfolded? The example of α-lactalbumin , 1987 .

[73]  P S Kim,et al.  Folding of a peptide corresponding to the alpha-helix in bovine pancreatic trypsin inhibitor. , 1989, Biochemistry.

[74]  Y. Myer.  Conformation of cytochromes. 3. Effect of urea, temperature, extrinsic ligands, and pH variation on the conformation of horse heart ferricytochrome c. , 1968, Biochemistry.

[75]  H. Scheraga,et al.  Experimental and theoretical aspects of protein folding. , 1975, Advances in protein chemistry.

[76]  Matthews Cr,et al.  Characterization of an early intermediate in the folding of the alpha subunit of tryptophan synthase by hydrogen exchange measurement. , 1985 .

[77]  N. Go.  Theoretical studies of protein folding. , 1983, Annual review of biophysics and bioengineering.

[78]  S. Harrison,et al.  Is there a single pathway for the folding of a polypeptide chain? , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[79]  K. Kuwajima,et al.  Thermodynamic characterization of partially denatured states in the denaturation process of bovine alpha-lactalbumin by inorganic denaturants. , 1977, Biochimica et biophysica acta.

[80]  O. Ptitsyn,et al.  Noncooperative temperature melting of a globular protein without specific tertiary structure: Acid form of bovine carbonic anhydrase B , 1985, Biopolymers.

[81]  J. J. Dougherty,et al.  Reoxidation of reduced bovine growth hormone from a stable secondary structure. , 1986, Biochemistry.

[82]  C. Chothia.  Principles that determine the structure of proteins. , 1984, Annual review of biochemistry.

[83]  G. Irace,et al.  Equilibrium evidence of non‐single step transition during guanidine unfolding of apomyoglobins , 1976, FEBS letters.

[84]  E. London,et al.  Similarity of the conformation of diphtheria toxin at high temperature to that in the membrane-penetrating low-pH state. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[85]  K. Kuwajima,et al.  Detection and characterization of the intermediate on the folding pathway of human alpha-lactalbumin. , 1978, Biochemistry.

[86]  D. Phillips,et al.  A possible three-dimensional structure of bovine alpha-lactalbumin based on that of hen's egg-white lysozyme. , 1969, Journal of molecular biology.

[87]  D I Stuart,et al.  Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme. , 1989, Journal of molecular biology.

[88]  O. Ptitsyn,et al.  α‐lactalbumin: compact state with fluctuating tertiary structure? , 1981, FEBS letters.

[89]  M. Kronman,et al.  Comparative fluorescence properties of bovine, goat, human and guinea pig alpha lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers. , 1980, Biophysical chemistry.

[90]  Matthews Cr.  Effect of point mutations on the folding of globular proteins. , 1987 .

[91]  E. Rowe,et al.  Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase B. , 1980, Biochemistry.

[92]  P. Privalov,et al.  Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride. , 1976, Biophysical chemistry.

[93]  K. Kuwajima,et al.  Folding of carp parvalbumin studied by equilibrium and kinetic circular dichroism spectra , 1988 .

[94]  A. Labhardt.  [7]Folding intermediates studied by circular dichroism , 1986 .

[95]  H. Scheraga,et al.  Effect of sequence‐specific interactions on the stability of helical conformations in polypeptides , 1988, Biopolymers.

[96]  S. Segawa,et al.  Characterization of the transition state of lysozyme unfolding. II. Effects of the intrachain crosslinking and the inhibitor binding on the transition state , 1984, Biopolymers.

[97]  Evidence for an initial fast nucleation process in the folding of human carbonic anhydrase I. , 2009, International journal of peptide and protein research.

[98]  G M Crippen,et al.  The tree structural organization of proteins. , 1978, Journal of molecular biology.

[99]  P. Privalov.  Stability of proteins: small globular proteins. , 1979, Advances in protein chemistry.

[100]  N. Kitabatake,et al.  Conformational changes in ovalbumin at acid pH. , 1988, Journal of biochemistry.

[101]  R. Norton,et al.  Denaturation of proteins. V. N.M.R. study of the arginine residues of lysozyme. , 2009, International journal of peptide and protein research.

[102]  C. Levinthal.  Are there pathways for protein folding , 1968 .

[103]  S. Sugai,et al.  Hydrophobic Domains of Maleic Acid Copolymers , 1985 .

[104]  T. Creighton,et al.  Unfolding and refolding of Staphylococcus aureus penicillinase by urea-gradient electrophoresis. , 1980, Journal of molecular biology.

[105]  Inter- and intramolecular interactions of -lactalbumin. XII. Changes in the environment of aromatic residues in the goat protein. , 1972, Biochimica et biophysica acta.

[106]  K. Kuwajima,et al.  α-Lactalbumin: A calcium metalloprotein , 1980 .

[107]  O. Ptitsyn.  Protein folding: Hypotheses and experiments , 1987 .

[108]  K. Kuwajima,et al.  Role of the Interaction between Ionizable Groups in the Folding of Bovine α-Lactalbumin , 1981 .

[109]  W. Pfeil.  Thermodynamics of α-lactalbumin unfolding , 1981 .

[110]  H. Scheraga,et al.  Hypothesis about the mechanism of protein folding. , 1977, Macromolecules.

[111]  F. M. Robbins,et al.  Inter- and intramolecular interactions of α-lactalbumin VIII. The alkaline conformational change , 1967 .

[112]  C. Tanford,et al.  Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions. , 1973, The Journal of biological chemistry.

[113]  K. Wong,et al.  Acid denaturation of bovine carbonic anhydrase B. , 1974, Biochemistry.

[114]  Y. Goto,et al.  Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chain. Kinetic role of the intrachain disulfide bond. , 1982, Journal of molecular biology.

[115]  S. Segawa,et al.  Characterization of the transition state of Lysozyme unfolding. I. Effect of protein‐solvent interactions on the transition state , 1984, Biopolymers.

[116]  T. Creighton.  Detection of folding intermediates using urea-gradient electrophoresis. , 1986, Methods in enzymology.

[117]  Y. Goto,et al.  Unfolding and refolding of the constant fragment of the immunoglobulin light chain. , 1982, Journal of molecular biology.

[118]  E. W. Kauffman,et al.  Equilibrium denaturation of pituitary- and recombinant-derived bovine growth hormone. , 1985, Biochemistry.

[119]  E. Haas,et al.  Reduced bovine pancreatic trypsin inhibitor has a compact structure. , 1988, Biochemistry.

[120]  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.

[121]  O. Ptitsyn,et al.  Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and ‘molten globule’ states , 1986 .

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

[123]  C. Mitchinson,et al.  Effects of sulphate and urea on the stability and reversible unfolding of beta-lactamase from Staphylococcus aureus. Implications for the folding pathway of beta-lactamase. , 1985, Journal of molecular biology.

[124]  W. DeGrado.  Design of peptides and proteins. , 1988, Advances in protein chemistry.