Forecasting the upper bound free energy difference between protein native-like structures
Jorge A. Vila
Physica A: Statistical Mechanics and its Applications, 2019, vol. 533, issue C
Abstract:
Using a combination of statistical thermodynamics and the Gershgorin theorem we computed, in the thermodynamic limit, a plausible value for the upper bound of the free energy difference between native-like structures of monomeric globular proteins. The validity of our result is discussed herein in terms of both the observed free-energy change between the native and denatured states and the micro stability free-energy values obtained from the observed micro-unfolding tendency of nine monomeric globular proteins.
Keywords: Free-energy; Protein; Native states; Gershgorin; Heuristic; Eigenvalues (search for similar items in EconPapers)
Date: 2019
References: Add references at CitEc
Citations:
Downloads: (external link)
http://www.sciencedirect.com/science/article/pii/S0378437119311975
Full text for ScienceDirect subscribers only. Journal offers the option of making the article available online on Science direct for a fee of $3,000
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:533:y:2019:i:c:s0378437119311975
DOI: 10.1016/j.physa.2019.122053
Access Statistics for this article
Physica A: Statistical Mechanics and its Applications is currently edited by K. A. Dawson, J. O. Indekeu, H.E. Stanley and C. Tsallis
More articles in Physica A: Statistical Mechanics and its Applications from Elsevier
Bibliographic data for series maintained by Catherine Liu ().