Characterization of the stable, acid‐induced, molten globule‐like state of staphylococcal nuclease
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[1] D. Engelman,et al. Truncated staphylococcal nuclease is compact but disordered. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[2] K. Kuwajima,et al. Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. , 1991, Biochemistry.
[3] R. L. Baldwin,et al. Early folding intermediate of ribonuclease A. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[4] A. Fersht,et al. Detection and characterization of a folding intermediate in barnase by NMR , 1990, Nature.
[5] A. Fink,et al. Mechanism of acid-induced folding of proteins. , 1990, Biochemistry.
[6] O. Ptitsyn,et al. Evidence for a molten globule state as a general intermediate in protein folding , 1990, FEBS letters.
[7] P. S. Kim,et al. Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.
[8] A. Fink,et al. Acid-induced folding of proteins. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[9] D. Shortle,et al. Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease. , 1989, Archives of biochemistry and biophysics.
[10] D. Shortle,et al. Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions. , 1989, Biochemistry.
[11] A. Fink,et al. Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. , 1989, Biochemistry.
[12] K. Kuwajima,et al. The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure , 1989, Proteins.
[13] S. Walter Englander,et al. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR , 1988, Nature.
[14] O. Ptitsyn,et al. Sequential mechanism of refolding of carbonic anhydrase B , 1987, FEBS letters.
[15] O. Ptitsyn,et al. An early intermediate of refolding α‐lactalbumin forms within 20 ms , 1987 .
[16] S Sugai,et al. Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism , 1987, FEBS letters.
[17] O. Ptitsyn. Protein folding: Hypotheses and experiments , 1987 .
[18] R. Jakobsen,et al. Effects of the Environment on the Structure of Adsorbed Proteins: Fourier Transform Infrared Spectroscopic Studies , 1987 .
[19] 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.
[20] 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.
[21] H. Susi,et al. Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.
[22] J. Bandekar,et al. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. , 1986, Advances in protein chemistry.
[23] K. Kuwajima,et al. Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin. , 1985, Biochemistry.
[24] R. J. Corbett,et al. Use of high-speed size-exclusion chromatography for the study of protein folding and stability. , 1984, Biochemistry.
[25] A. Wada,et al. ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains , 1983, FEBS letters.
[26] D. Worah,et al. Binding of recrystallized and chromatographically purified 8-anilino-1-naphthalenesulfonate to Escherichia coli lac repressor. , 1978, Biochemistry.