A model for the thermodynamics of globular proteins

Alex Hansen, Mogens H Jensen, Kim Sneppen and Giovanni Zocchi

Physica A: Statistical Mechanics and its Applications, 1999, vol. 270, issue 1, 278-287

Abstract: We review a statistical mechanics treatment of the stability of globular proteins based on a simple model Hamiltonian taking into account protein self-interactions and protein–water interactions. The model contains both hot and cold folding transitions. In addition it predicts a critical point at a given temperature and chemical potential of the surrounding water. The universality class of this critical point is new.

Keywords: Protein folding; Protein thermodynamics; Cold denaturation; Folding pathways (search for similar items in EconPapers)
Date: 1999
References: View complete reference list from CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
http://www.sciencedirect.com/science/article/pii/S0378437199001314
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:270:y:1999:i:1:p:278-287

DOI: 10.1016/S0378-4371(99)00131-4

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 ().