DOI: 10.1016/j.jmb.2005.05.062. Interpretation of Protein Folding ψ Values

Interpretation of Protein Folding ψ Values

10.1016/j.jmb.2005.05.062

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Bodenreider, C., & Kiefhaber, T. (2005). Interpretation of Protein Folding Ï Values. Journal of Molecular Biology, 351(2), 393â401.

Authors 2

Christophe Bodenreider (first)
Thomas Kiefhaber (additional)

References 37 Referenced 19

10.1126/science.117.3039.340 / Science / Parameters for the description of transition states by Leffler (1953)
10.1021/ja00466a030 / J. Am. Chem. Soc. / On the characterization of transition states by structure-reactivity coefficients by Jencks (1977)
10.1016/S0301-4622(02)00294-6 / Biophys. Chem. / Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding by Sánchez (2003)
10.1016/S0022-2836(03)00171-2 / J. Mol. Biol. / Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states by Sánchez (2003)
{'key': '10.1016/j.jmb.2005.05.062_bib5', 'first-page': '411', 'article-title': 'Characterization of protein folding barriers with rate-equilibrium free-energy relationships', 'volume': 'vol. 1', 'author': 'Kiefhaber', 'year': '2005'} / Characterization of protein folding barriers with rate-equilibrium free-energy relationships by Kiefhaber (2005)
10.1021/ja01607a027 / J. Am. Chem. Soc. / A correlation of reaction rates by Hammond (1955)
10.1021/cr00070a001 / Chem. Rev. / A primer for the Bema Hapothle. An empirical approach to the characterization of changing transition-state structures by Jencks (1985)
{'key': '10.1016/j.jmb.2005.05.062_bib8', 'series-title': 'Rates and Equilibria of Organic Reactions', 'author': 'Leffler', 'year': '1963'} / Rates and Equilibria of Organic Reactions by Leffler (1963)
10.1006/jmbi.2000.4399 / J. Mol. Biol. / Apparent two-state tendamistat folding is a sequential process along a defined route by Bachmann (2001)
10.1016/S0022-2836(02)01230-5 / J. Mol. Biol. / Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding by Sánchez (2003)
10.1021/ed052p76 / J. Chem. Ed. / The use and misuse of the Hammond postulate by Farcasiu (1975)
10.1016/S0065-3233(08)60241-7 / Advan. Protein Chem. / Protein denaturation. Part C. Theoretical models for the mechanism of denaturation by Tanford (1970)
10.1002/pro.5560041020 / Protein Sci. / Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding by Myers (1995)
10.1021/bi00015a001 / Biochemistry / Evidence for a molten globule-like transition state in protein folding from determination of activation volumes by Vidugiris (1995)
10.1073/pnas.97.1.17 / Proc. Natl Acad. Sci. USA / Denaturant-induced movement of the transition state of protein folding revealed by high pressure stopped-flow measurements by Pappenberger (2000)
10.1016/0014-5793(76)80132-9 / FEBS Letters / Temperature-dependence of the kinetics of folding of chymotrypsinogen A by Pohl (1976)
10.1021/bi962090j / Biochemistry / Thermodynamic characterization of an extreemely rapid protein folding reaction by Schindler (1996)
10.1021/bi970594r / Biochemistry / Effect of pre-formed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for β-sheet formation by Schönbrunner (1997)
10.1073/pnas.94.20.10636 / Proc. Natl Acad. Sci. USA / Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability by Scalley (1997)
10.1006/jmbi.1998.2246 / J. Mol. Biol. / Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9 by Kuhlman (1998)
10.1006/jmbi.2001.4873 / J. Mol. Biol. / The folding mechanism of a beta-sheet: the WW domain by Jäger (2001)
10.1016/0076-6879(87)54092-7 / Methods Enzymol. / Effect of point mutations on the folding of globular proteins by Matthews (1987)
10.1016/0022-2836(92)90561-W / J. Mol. Biol. / The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding by Fersht (1992)
10.1016/0022-2836(89)90500-7 / J. Mol. Biol. / Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin by Kuwajima (1989)
10.1016/0022-2836(91)80188-Z / J. Mol. Biol. / Mapping transition states of protein unfolding by protein engineering of ligand-binding sites by Sancho (1991)
10.1006/jmbi.1996.0647 / J. Mol. Biol. / Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways by Tan (1996)
10.1016/S0022-2836(02)00015-3 / J. Mol. Biol. / pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9 by Sato (2002)
10.1016/j.jmb.2004.10.023 / J. Mol. Biol. / Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state of protein folding by Horng (2005)
10.1038/nsb723 / Nature Struct. Biol. / Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil by Krantz (2001)
10.1016/j.jmb.2004.01.018 / J. Mol. Biol. / Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis by Krantz (2004)
10.1073/pnas.0407683101 / Proc. Natl Acad. Sci. USA / Differences in the folding transition state of ubiquitin indicated by ϕ and ψ analysis by Sosnick (2004)
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10.1021/bi00461a025 / Biochemistry / pH-induced denaturation of proteins: a single salt bridge contributes 4–5kcal/mol to the free energy of folding of T4 lysozyme by Anderson (1990)
10.1006/jmbi.1997.1030 / J. Mol. Biol. / Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate by Wildegger (1997)
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10.1016/j.jmb.2003.10.016 / J. Mol. Biol. / Origin of unusual phi-values in protein folding: evidence against specific nucleation sites by Sánchez (2003)

Dates

Type	When
Created	20 years, 2 months ago (June 15, 2005, 3:43 a.m.)
Deposited	6 years, 7 months ago (Jan. 25, 2019, 12:54 p.m.)
Indexed	1 year, 4 months ago (April 10, 2024, 9:58 a.m.)
Issued	20 years ago (Aug. 1, 2005)
Published	20 years ago (Aug. 1, 2005)
Published Print	20 years ago (Aug. 1, 2005)

Funders 0

None

BibTeX

@article{Bodenreider_2005, title={Interpretation of Protein Folding ψ Values}, volume={351}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2005.05.062}, DOI={10.1016/j.jmb.2005.05.062}, number={2}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Bodenreider, Christophe and Kiefhaber, Thomas}, year={2005}, month=aug, pages={393–401} }

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