| Literature DB >> 20055447 |
Angel L Pey1, David Rodriguez-Larrea, Jose A Gavira, Bertrand Garcia-Moreno, Jose M Sanchez-Ruiz.
Abstract
Recent work has shown that proteins can tolerate hydrophobic-to-ionizable-residue mutations. Here, we provide experimental evidence that the essential properties (pK value, protonation state, local dynamics) of buried ionizable groups in proteins can be efficiently modulated through the rational design of the surface charge distribution, thus paving the way for the protein engineering exploitation of charge burial.Entities:
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Year: 2010 PMID： 20055447 DOI： 10.1021/ja909298v
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419