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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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Bibliografiske detaljer
Main Authors: Isom, Daniel G., Castañeda, Carlos A., Cannon, Brian R., Velu, Priya D., García-Moreno E., Bertrand
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 2010
Fag:
Online adgang: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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