Evidence for a molten globule state as a general intermediate in protein folding

We propose that the formation of the transient molten globule state occurs early on the pathway of folding of all globular proteins.

[1]  B. Robson,et al.  Analysis of the code relating sequence to conformation in proteins: possible implications for the mechanism of formation of helical regions. , 1971, Journal of molecular biology.

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

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

[4]  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.

[5]  P. Wingfield,et al.  Conformation, stability, and folding of interleukin 1 beta. , 1987, Biochemistry.

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

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

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

[9]  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.

[10]  [Self-organization of the myoglobin molecule]. , 1973 .

[11]  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.

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

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

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

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

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

[17]  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.

[18]  R. Pain,et al.  Conformation of a stable intermediate on the folding pathway of Staphylococcus aureus penicillinase. , 1978, Biochimica et biophysica acta.

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

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

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

[22]  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.

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

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