
doi: 10.1002/prot.24045
pmid: 22383276
AbstractThe 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.
Models, Molecular, Protein Conformation, Amino Acid Motifs, Hydrogen Bonding, Amino Acids, Databases, Protein, Peptides
Models, Molecular, Protein Conformation, Amino Acid Motifs, Hydrogen Bonding, Amino Acids, Databases, Protein, Peptides
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