Keywords
Monte Carlo methods, Thermodynamic properties, Dichroism, Optical tweezers, Chemical bonding, Denaturation (biochemistry), Atomic force microscopy, Protein folding, Protein structure, Mutagenesis
Abstract
Two different classes of experimental techniques exist by which protein folding mechanisms are ascertained. The first class, of which circular dichroism is an example, probes thermally-induced folding. The second class, which includes atomic force microscopy and optical tweezers, measures mechanically-induced folding. In this article, we investigate if proteins fold/unfold via the same mechanisms both thermally and mechanically. We do so using Ribonuclease H, a protein that has been shown to fold through a three-state mechanism using both types of experimental techniques. A detailed, molecular-level description of the states involved in thermal and mechanical folding shows that mechanisms for both types are globally similar, but small difference exist in the most unfolded conformations. Comparison to previous work suggests a universal folding behavior for proteins with a core helical bundle.
Original Publication Citation
T. J. Schmitt, J. Clark, and T. A. Knotts IV, Thermal and Mechanical Multistate Folding of RNAse H, J. Chem. Phys., 131, 235101 (2009).
BYU ScholarsArchive Citation
Knotts, Thomas A.; Schmitt, Terry J.; and Clark, Jonathan E., "Thermal and Mechanical Multistate Folding of RNAse H" (2009). Faculty Publications. 7709.
https://scholarsarchive.byu.edu/facpub/7709
Document Type
Peer-Reviewed Article
Publication Date
2009-12-21
Publisher
American Institute of Physics
Language
English
College
Ira A. Fulton College of Engineering
Department
Chemical Engineering
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