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Ion–dipole interactions and their functions in proteins
Author(s) -
Sippel Katherine H.,
Quiocho Florante A.
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2685
Subject(s) - ion , dipole , chemistry , macromolecule , protein data bank (rcsb pdb) , chemical physics , protein data bank , hydrogen bond , protein structure , computational biology , biophysics , computational chemistry , biology , biochemistry , molecule , organic chemistry
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.