The ST pinch: A side chain‐to‐side chain hydrogen‐bonded motif | Zendy

Bomar Martha G. | Zendy; Raghavender Upadhyayula S. | Zendy; Spindel Alexander W. I. | Zendy; Kodukula Krishna | Zendy; Galande Amit K. | Zendy

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The ST pinch: A side chain‐to‐side chain hydrogen‐bonded motif

Author(s) -

Bomar Martha G.,

Raghavender Upadhyayula S.,

Spindel Alexander W. I.,

Kodukula Krishna,

Galande Amit K.

Publication year - 2012

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.24045

Subject(s) - side chain , chemistry , hydrogen bond , linker , residue (chemistry) , structural motif , crystallography , protein structure , stereochemistry , molecule , biochemistry , organic chemistry , computer science , polymer , operating system

The ST Pinch is a 12‐membered hydrogen‐bonded motif (Ser/Thr‐Xaa‐Ser/Thr) involving the side chain oxygen atoms of two Ser/Thr residues. We identified the ST Pinch in 104 proteins in a database containing high‐resolution crystal structures. Conformational analysis of the ST Pinch in these proteins points to specific preferences for the Xaa residue and a high propensity of this residue to adopt positive φ angles. Our results suggest that this motif serves as a linker of secondary structural elements within proteins and is a new addition to the existing list of short hydrogen bond‐stabilized motifs in proteins. Proteins 2012;. © 2012 Wiley Periodicals, Inc.

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