Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 4, Pages 1218-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja909298v
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Funding
- Spanish Ministry of Education and Science [BIO2006-07332]
- Junta de Andalucia [CVI-771]
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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.
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