Crossref
journal-article
Elsevier BV
Journal of Molecular Biology (78)
References
51
Referenced
56
10.1021/bi00199a029
/ Biochemistry / Specific nucleus as the transition state for protein folding by Abkevich (1994)10.1021/bi00147a006
/ Biochemistry / Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal Protein G by Alexander (1992)10.1002/prot.340210302
/ Proteins: Struct. Funct. Genet. / Funnels, pathways, and the energy landscape of protein folding by Bryngelson (1995)10.1021/bi00155a024
/ Biochemistry / Kinetic resolution of peptide bond and side-chain far-UV CD during folding of HEWL by Chaffotte (1992)10.1073/pnas.94.5.1779
/ Proc. Natl Acad. Sci. USA / Submillisecond protein folding kinetics studied by ultrarapid mixing by Chan (1997)10.1073/pnas.87.16.6388
/ Proc. Natl Acad. Sci. USA / Origins of structure in globular proteins by Chan (1990)10.1006/jmbi.1996.0491
/ J. Mol. Biol. / A lysozyme folding intermediate revealed by solution X-ray scattering by Chen (1996)10.1042/bj2700001
/ Biochem. J. / Protein folding by Creighton (1990)10.1016/0167-4838(91)90571-G
/ Biochim. Biophys. Acta / Acid denatured apo-cytochrome c is a random coil by Damaschun (1991)10.1021/bi00203a019
/ Biochemistry / Kinetics of folding of guanidine-denatured hen egg white lysozyme and carboxymethyl (Cys6, Cys127)-lysozyme by Denton (1994)10.1021/bi00483a001
/ Biochemistry / Dominant forces in protein folding by Dill (1990)10.1016/0959-440X(92)90169-8
/ Curr. Opin. Struct. Biol. / Unfolded proteins, compact states and molten globules by Dobson (1992)10.1006/jmbi.1995.0668
/ J. Mol. Biol. / Partially folded states of proteins by Doniach (1995)10.1016/S0006-3495(93)81124-X
/ Biophys. J. / Evidence of an associative intermediate on the myoglobin refolding pathway by Eliezer (1993)10.1126/science.270.5235.487
/ Science / The radius of gyration of an apomyoglobin folding intermediate by Eliezer (1995)10.1021/bi00145a003
/ Biochemistry / Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy by Elöve (1992)10.1016/0959-440X(95)80012-P
/ Curr. Opin. Struct. Biol. / Characterizing transition states in protein folding by Fersht (1995)10.1073/pnas.93.19.10167
/ Proc. Natl Acad. Sci. USA / Packing at the protein-water interface by Gerstein (1996)10.1006/jmbi.1995.0351
/ J. Mol. Biol. / The volume of atoms on the protein surface by Gerstein (1995)10.1016/S1359-0278(96)00057-0
/ Folding Design / Structure of very early protein folding intermediates by Gladwin (1996){'key': '10.1006/jmbi.1997.1514_BIB21', 'series-title': 'Small Angle X-ray Scattering', 'author': 'Glatter', 'year': '1982'}
/ Small Angle X-ray Scattering by Glatter (1982)10.1021/bi00009a031
/ Biochemistry / Protein folding with rapidly exchangable amide protons contain authentic hydrogen-bonded secondary structure by Guijarro (1995)10.1002/bip.360360108
/ Biopolymers / Kinetics of protein folding by Guo (1995)10.1016/0076-6879(92)10010-B
/ Methods In Enzymology / Singular value decomposition by Henry (1992)10.1021/bi00183a026
/ Biochemistry / Tertiary interactions in the folding pathway of hen lysozyme by Itzhaki (1994)10.1021/bi00107a010
/ Biochemistry / Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition by Jackson (1991)10.1021/bi00508a006
/ Biochemistry / Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme by Kato (1981)10.1021/bi00530a007
/ Biochemistry / Identification and characterization of the direct folding process of hen egg-white lysozyme by Kato (1982)10.1073/pnas.92.20.9029
/ Proc. Natl Acad. Sci. USA / Kinetic traps in lysozyme folding by Kiefhaber (1995)10.1021/bi9702391
/ Biochemistry / Direct measurement of nucleation and growth rates in lysozyme folding by Kiefhaber (1997)10.1146/annurev.bi.51.070182.002331
/ Annu. Rev. Biochem. / Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding by Kim (1982)10.1146/annurev.bi.59.070190.003215
/ Annu. Rev. Biochem. / Intermediates in the folding reactions of small proteins by Kim (1990)10.1002/prot.340060202
/ Proteins: Struct. Funct. Genet. / The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure by Kuwajima (1989)10.1021/bi00325a010
/ Biochemistry / Comparison of the transient folding intermediates in lysozyme and α-lactalbumin by Kuwajima (1985)10.1016/0022-2836(71)90324-X
/ J. Mol. Biol. / The interpretation of protein structures by Lee (1971){'key': '10.1006/jmbi.1997.1514_BIB36', 'series-title': 'Numerical Recipes in C: The Art of Scientific Computing', 'author': 'Press', 'year': '1992'}
/ Numerical Recipes in C: The Art of Scientific Computing by Press (1992)10.1016/0014-5793(90)80143-7
/ FEBS Letters / Evidence for a molten globule state as a general intermediate in protein folding by Ptitsyn (1990)10.1038/358302a0
/ Nature / The folding of hen lysozyme involves partially structured intermediates and multiple pathways by Radford (1992)10.1038/369248a0
/ Nature / How does a protein fold? by Sali (1994)10.1038/nsb0895-663
/ Nature Struct. Biol. / Extremely rapid protein folding in the absence of intermediates by Schindler (1995)10.1021/bi00289a013
/ Biochemistry / Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates by Schmid (1983)10.1006/jmbi.1997.0960
/ J. Mol. Biol. / Folding of the disulfide-bonded β-sheet protein tendamistat by Schönbrunner (1997)10.1038/nsb0394-149
/ Nature Struct. Biol. / The barriers in protein folding by Sosnick (1994)10.1016/0022-2836(73)90322-7
/ Mol. Biol. / Kinetics of unfolding and refolding of proteins. 3. Results for lysozyme by Tanford (1973){'key': '10.1006/jmbi.1997.1514_BIB45', 'first-page': '1457', 'article-title': 'From minimal models to real proteins', 'volume': '5', 'author': 'Thirumalai', 'year': '1995', 'journal-title': 'J. Physique'}
/ J. Physique / From minimal models to real proteins by Thirumalai (1995)10.1063/1.1140768
/ Rev. Sci. Instr. / Stopped-flow apparatus for X-ray scattering at subzero temperature by Tsuruta (1989)10.1126/science.8493553
/ Science / Kinetics of folding of the all-β-sheet protein interleukin-1β by Varley (1993)10.1021/bi00174a022
/ Biochemistry / Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition by Viguera (1994)10.1021/bi00046a017
/ Biochemistry / Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2 by Villegas (1995)10.1006/jmbi.1997.1030
/ J. Mol. Biol. / Three-state model for lysozyme folding by Wildegger (1997)10.1073/pnas.92.21.9801
/ Proc. Natl Acad. Sci. USA / Simple model of protein folding kinetics by Zwanzig (1995)
Dates
Type | When |
---|---|
Created | 22 years, 11 months ago (Sept. 18, 2002, 3:24 p.m.) |
Deposited | 2 years, 5 months ago (March 30, 2023, 10:13 p.m.) |
Indexed | 1 year, 1 month ago (Aug. 5, 2024, 7:23 a.m.) |
Issued | 27 years, 7 months ago (Feb. 1, 1998) |
Published | 27 years, 7 months ago (Feb. 1, 1998) |
Published Print | 27 years, 7 months ago (Feb. 1, 1998) |
@article{Chen_1998, title={Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering}, volume={276}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.1997.1514}, DOI={10.1006/jmbi.1997.1514}, number={1}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Chen, Lingling and Wildegger, Gudrun and Kiefhaber, Thomas and Hodgson, Keith O and Doniach, Sebastian}, year={1998}, month=feb, pages={225–237} }