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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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Bibliografski detalji
Glavni autori: Isom, Daniel G., Castañeda, Carlos A., Cannon, Brian R., Velu, Priya D., García-Moreno E., Bertrand
Format: Artigo
Jezik:Inglês
Izdano: National Academy of Sciences 2010
Teme:
Online pristup: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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