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Charges in the hydrophobic interior of proteins

Charges are inherently incompatible with hydrophobic environments. Presumably for this reason, ionizable residues are usually excluded from the hydrophobic interior of proteins and are found instead at the surface, where they can interact with bulk water. Paradoxically, ionizable groups buried in th...

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Библиографические подробности
Главные авторы: Isom, Daniel G., Castañeda, Carlos A., Cannon, Brian R., Velu, Priya D., García-Moreno E., Bertrand
Формат: Artigo
Язык:Inglês
Опубликовано: National Academy of Sciences 2010
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2941338/
https://ncbi.nlm.nih.gov/pubmed/20798341
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1004213107
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