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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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Detalhes bibliográficos
Main Authors: Isom, Daniel G., Castañeda, Carlos A., Cannon, Brian R., Velu, Priya D., García-Moreno E., Bertrand
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2010
Assuntos:
Acesso em linha: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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