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• W2071701532 abstract "Abstract The geometry of interactions of planar residues is nonrandom in protein tertiary structures and gives rise to conventional, as well as nonconventional (XH···π, XH···O, where X = C, N, or O) hydrogen bonds. Whether a similar geometry is maintained when the interaction is across the protein–protein interface is addressed here. The relative geometries of interactions involving planar residues, and the percentage of contacts giving rise to different types of hydrogen bonds are quite similar in protein structures and the biological interfaces formed by protein chains in homodimers and protein–protein heterocomplexes—thus pointing to the similarity of chemical interactions that occurs during protein folding and binding. However, the percentage is considerably smaller in the nonspecific and nonphysiological interfaces that are formed in crystal lattices of monomeric proteins. The CH···O interaction linking the aromatic and the peptide groups is quite common in protein structures as well as the three types of interfaces. However, as the interfaces formed by crystal contacts are depleted in aromatic residues, the weaker hydrogen bond interactions would contribute less toward their stability. Proteins 2007; © 2007 Wiley‐Liss, Inc." @default.
• W2071701532 created "2016-06-24" @default.
• W2071701532 creator A5000031273 @default.
• W2071701532 creator A5055063575 @default.
• W2071701532 creator A5088368426 @default.
• W2071701532 date "2007-01-12" @default.
• W2071701532 modified "2023-10-18" @default.
• W2071701532 title "Interaction geometry involving planar groups in protein-protein interfaces" @default.
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• W2071701532 doi "https://doi.org/10.1002/prot.21244" @default.
• W2071701532 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17221868" @default.
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