@Article{CiCP-13-90,
author = {Mihir S. Date and Brian N. Dominy},
title = {Modeling the Influence of Salt on the Hydrophobic Effect and Protein Fold Stability},
journal = {Communications in Computational Physics},
year = {2013},
volume = {13},
number = {1},
pages = {90--106},
abstract = {<p style="text-align: justify;">Salt influences protein stability through electrostatic mechanisms as well as through nonpolar Hofmeister effects. In the present work, a continuum solvation based model is developed to explore the impact of salt on protein stability. This model relies on a traditional Poisson-Boltzmann (PB) term to describe the polar or electrostatic effects of salt, and a surface area dependent term containing a salt concentration dependent microscopic surface tension function to capture the non-polar Hofmeister effects. The model is first validated against a series of cold-shock protein variants whose salt-dependent protein fold stability profiles have been previously determined experimentally. The approach is then applied to HIV-1 protease in order to explain an experimentally observed enhancement in stability and activity at high (1M) NaCl concentration. The inclusion of the salt-dependent non-polar term brings the model into quantitative agreement with experiment, and provides the basis for further studies into the impact of ionic strength on protein structure, function, and evolution.&nbsp;</p>},
issn = {1991-7120},
doi = {https://doi.org/10.4208/cicp.290711.121011s},
url = {http://global-sci.org/intro/article_detail/cicp/7213.html}
}