DOI: 10.1073/pnas.90.2.439. Protein folding--what's the question?

10.1073/pnas.90.2.439

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

The folding reactions of many small, globular proteins exhibit two-state kinetics, in which the folded and unfolded states interconvert readily without observable intermediates. Typically, the free energy difference, delta G, between the native and denatured states of such a protein is quite small, lying in the range of approximately -5 to -15 kcal/mol. We point out that, under these circumstances, a population of native-like molecules will persist, even in the presence of mutations sufficiently destabilizing to change the sign of delta G. Therefore, it is not energy per se that determines conformation. A corollary to this argument is that specificity--not stability--would be the more informative focus in future folding studies.

Bibliography

Lattman, E. E., & Rose, G. D. (1993). Protein folding--whatâs the question? Proceedings of the National Academy of Sciences, 90(2), 439â441.

Authors 2

E E Lattman (first)
G D Rose (additional)

References 0 Referenced 139

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 8:32 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 1:47 p.m.)
Indexed	2 weeks, 4 days ago (Aug. 19, 2025, 6:36 a.m.)
Issued	32 years, 7 months ago (Jan. 15, 1993)
Published	32 years, 7 months ago (Jan. 15, 1993)
Published Online	32 years, 7 months ago (Jan. 15, 1993)
Published Print	32 years, 7 months ago (Jan. 15, 1993)

Funders 0

None

BibTeX

@article{Lattman_1993, title={Protein folding--what’s the question?}, volume={90}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.90.2.439}, DOI={10.1073/pnas.90.2.439}, number={2}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Lattman, E E and Rose, G D}, year={1993}, month=jan, pages={439–441} }

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