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Ion-dipole interactions and their functions in proteins.

ABSTRACT: Ion-dipole interactions in biological macromolecules are formed between atomic or molecular ions and neutral protein dipolar groups through either hydrogen bond or coordination. Since their discovery 30 years ago, these interactions have proven to be a frequent occurrence in protein structures, appearing in everything from transporters and ion channels to enzyme active sites to protein-protein interfaces. However, their significance and roles in protein functions are largely underappreciated. We performed PDB data mining to identify a sampling of proteins that possess these interactions. In this review, we will define the ion-dipole interaction and discuss several prominent examples of their functional roles in nature.

SUBMITTER: Sippel KH

PROVIDER: S-EPMC4500305 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature

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Ion-dipole interactions and their functions in proteins.

Sippel Katherine H KH Quiocho Florante A FA

Protein science : a publication of the Protein Society 20150501 7

Ion-dipole interactions in biological macromolecules are formed between atomic or molecular ions and neutral protein dipolar groups through either hydrogen bond or coordination. Since their discovery 30 years ago, these interactions have proven to be a frequent occurrence in protein structures, appearing in everything from transporters and ion channels to enzyme active sites to protein-protein interfaces. However, their significance and roles in protein functions are largely underappreciated. We ...[more]

PMID: 25866296

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