Initial hydrophobic collapse is not necessary for folding RNase A
Tài liệu tham khảo
Nath, 1997, How do proteins fold?, Curr. Sci, 72, 180
Levitt, 1975, Computer simulation of protein folding, Nature, 253, 694, 10.1038/253694a0
Dill, 1985, Theory for the folding and stability of globular proteins, Biochemistry, 24, 1501, 10.1021/bi00327a032
Chan, 1990, Origins of structure in globular proteins, Proc. Natl Acad. Sci. USA, 87, 6388, 10.1073/pnas.87.16.6388
Ptitsyn, 1973, Stages in the mechanism of self-organization of protein molecules, Dokl. Akad. Nauk. SSSR, 210, 1213
Kim, 1982, Specific intermediates in the folding reactions of small proteins and the mechanism of folding, Annu. Rev. Biochem, 51, 459, 10.1146/annurev.bi.51.070182.002331
Karplus, 1994, Protein folding dynamics: the diffusion-collision model and experimental data, Protein Sci, 3, 650, 10.1002/pro.5560030413
Kuwajima, 1996, Stopped-Flow Circular Dichroism, 159
Reinstädler, 1996, Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy, Biochemistry, 35, 15822, 10.1021/bi961810j
Dyson, 1996, Insights into protein folding from NMR, Annu. Rev. Phys. Chem, 47, 369, 10.1146/annurev.physchem.47.1.369
Eliezer, 1993, The radius of gyration of an apomyoglobin folding intermediate, Science, 270, 487, 10.1126/science.270.5235.487
Semisotnov, 1996, Protein globularization during folding: a study by synchrotron small angle X-ray scattering, J. Mol. Biol, 262, 559, 10.1006/jmbi.1996.0535
Damaschun, 1998, Denatured states of yeast phosphoglycerate kinase, Biochemistry (Moscow), 63, 259
Gast, 1997, Stopped flow dynamic light scattering as a method to monitor compaction during protein folding, Eur. Biophys. J, 25, 211, 10.1007/s002490050033
Brandts, 1975, Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues, Biochemistry, 14, 4953, 10.1021/bi00693a026
Houry, 1994, A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathways, Biochemistry, 33, 2516, 10.1021/bi00175a022
Garel, 1973, Both the fast and slow refolding reactions of ribonuclease A yield native enzyme, Proc. Natl Acad. Sci. USA, 70, 3347, 10.1073/pnas.70.12.3347
Houry, 1996, Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerization, Biochemistry, 35, 11719, 10.1021/bi960745a
Cook, 1979, Role of proline isomerization in folding of ribonuclease A at low temperatures, Proc. Natl Acad. Sci. USA, 76, 6157, 10.1073/pnas.76.12.6157
Schmid, 1981, A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A, Eur. J. Biochem, 114, 111, 10.1111/j.1432-1033.1981.tb06180.x
Udgaonkar, 1988, NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A, Nature, 335, 694, 10.1038/335694a0
Udgaonkar, 1990, Early folding intermediate of ribonuclease A, Proc. Natl Acad. Sci. USA, 87, 8197, 10.1073/pnas.87.21.8197
Udgaonkar, 1995, Nature of the early folding intermediate of ribonuclease A, Biochemistry, 34, 4088, 10.1021/bi00012a027
Schmid, 1983, Mechanism of folding of ribonuclease A. Slow folding is a sequential reaction via structural intermediates, Biochemistry, 22, 4690, 10.1021/bi00289a013
Gast, 1992, Application of dynamic light scattering to studies of protein folding kinetics, Eur. Biophys. J, 5, 357
Pecorari, 1996, Occurrence of transient multimeric species during the refolding of a monomeric protein, J. Biol. Chem, 271, 5270, 10.1074/jbc.271.9.5270
Silow, 1997, Transient aggregates in protein folding are easily mistaken for folding intermediates, Proc. Natl Acad. Sci. USA, 94, 6084, 10.1073/pnas.94.12.6084
Gast, 1986, Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and ‘molten globule’ states, Int. J. Biol. Macromol, 8, 231, 10.1016/0141-8130(86)90032-2
Kataoka, 1997, Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering, Protein Sci, 6, 422, 10.1002/pro.5560060219
Brahms, 1980, Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism, J. Mol. Biol, 138, 149, 10.1016/0022-2836(80)90282-X
Scholtz, 1993, Perchlorate-induced denaturation of ribonuclease A: investigation of possible folding intermediates, Biochemistry, 32, 4604, 10.1021/bi00068a017
Guijarro, 1995, Protein folding intermediates with rapidly exchangeable amide protons contain authentic hydrogen-bonded secondary structures, Biochemistry, 34, 2998, 10.1021/bi00009a031
Hamada, 1996, Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein, Nat. Struct. Biol, 3, 868, 10.1038/nsb1096-868
Neira, 1997, Folding studies on ribonuclease A, a model protein, Fold. Des, 2, R1, 10.1016/S1359-0278(97)00001-1
Levitt, 1981, Effect of proline residues in protein folding, J. Mol. Biol, 145, 251, 10.1016/0022-2836(81)90342-9
Agashe, 1995, Initial hydrophobic collapse in the folding of barstar, Nature, 377, 754, 10.1038/377754a0
Arai, 1996, Rapid formation of a molten globule intermediate in refolding of α-lactalbumin, Fold. Des, 1, 275, 10.1016/S1359-0278(96)00041-7
Jacob, 1997, Diffusion control in an elementary protein folding reaction, Proc. Natl Acad. Sci. USA, 94, 5622, 10.1073/pnas.94.11.5622
Schönbrunner, 1997, Folding of the disulfide-bonded β-sheet protein tendamistat: rapid two-state folding without hydrophobic collapse, J. Mol. Biol, 268, 526, 10.1006/jmbi.1997.0960
Pace, 1989, Measuring the conformational stability of a protein, 311
Johnson, 1990, Protein secondary structure and circular dichroism: a practical guide, Proteins, 7, 205, 10.1002/prot.340070302
Provencher, 1982, CONTIN: a general purpose constrained regularization program for inverting noisy linear algebraic and integral equations, Comput. Phys. Commun, 27, 229, 10.1016/0010-4655(82)90174-6
Wlodawer, 1988, Structure of phosphate-free ribonuclease A refined at 1.26 å, Biochemistry, 27, 2705, 10.1021/bi00408a010
Evans, 1993, SETOR: hardware lighted three-dimensional solid model representations of macromolecules, J. Mol. Graphics, 11, 134, 10.1016/0263-7855(93)87009-T