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Atomistic mechanism of protein denaturation by urea
Published in American Chemical Society
PMID: 18543983
Volume: 112
Issue: 26
Pages: 7903 - 7908
Effects of urea on protein stability have been studied from all-atom molecular dynamics simulations of ubiquitin, G311 protein, and immunoglobulin binding domain (B1) of streptococcal protein G (GB1) in water and 8 M aqueous urea solution. The mechanism of the change in the solvent environment and the early events in protein unfolding by urea have been identified with emphasis on the change in the interactions of hydrophilic and hydrophobic parts of the protein by calculating the potential of mean force (PMF). Urea replaces the protein-protein and protein-water contacts by forming stronger contacts with the protein, which is indicated by the longer survival times of the protein-urea hydrogen bonds. © 2008 American Chemical Society.
About the journal
JournalData powered by TypesetJournal of Physical Chemistry B
PublisherData powered by TypesetAmerican Chemical Society
Open AccessNo