Work

Protein folding--what's the question?

Year: 1993

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.90.2.439

Authors: E E Lattman, G D Rose

Institutions: Johns Hopkins University, Johns Hopkins Medicine

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: G1138742246, G3121916556, SELF RECOGNITION IN GLOBULAR PROTEINS, STRUCTURE/INTERACTIONS OF ACTINS &ACTIN BINDING PROTEIN