Thirumalai, D. and O'Brien, Edward P. and Morrison, Greg and Hyeon, Changbong Theoretical Perspectives on Protein Folding. Annual Review of Biophysics, 39 (1). pp. 159-183. ISSN 1936-122X (2010)Full text not available from this repository.
Understanding how monomeric proteins fold under in vitro conditions is crucial to describing their functions in the cellular context. Significant advances in theory and experiments have resulted in a conceptual framework for describing the folding mechanisms of globular proteins. The sizes of proteins in the denatured and folded states, cooperativity of the folding transition, dispersions in the melting temperatures at the residue level, and timescales of folding are, to a large extent, determined by N, the number of residues. The intricate details of folding as a function of denaturant concentration can be predicted by using a novel coarse-grained molecular transfer model. By watching one molecule fold at a time, using single-molecule methods, investigators have established the validity of the theoretically anticipated heterogeneity in the folding routes and the N-dependent timescales for the three stages in the approach to the native state. Despite the successes of theory, of which only a few examples are documented here, we conclude that much remains to be done to solve the protein folding problem in the broadest sense.
|Uncontrolled Keywords:||universality in protein folding, role of protein length, molecular transfer model, single molecule force spectroscopy|
|Subjects:||Q Science > QC Physics
Q Science > QH Natural history > QH301 Biology
|Research Area:||Economics and Institutional Change|
|Depositing User:||Ms T. Iannizzi|
|Date Deposited:||04 Oct 2013 10:11|
|Last Modified:||21 Nov 2013 12:19|
Actions (login required)