Serine and Threonine Residues Bend α-Helices in the χ1 = g− Conformation

By J. Ballesteros, X. Deupí, M. Olivella, E. Haaksma, L. Pardo. 2000

160 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6afe1a93060e5781b9aaaa9695583b1cc9dee08d

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In Molecular Biology

1. M. Dubocovich

Citations in the corpus

• Ser and Thr Residues Modulate the Conformation of Pro-Kinked Transmembrane α-Helices (2004, background): “Besides the important role of Pro residues (Sansom and Weinstein, 2000), Ser and Thr residues also induce helical distortions of possible functional importance (Ballesteros et al., 2000).”
• International Union of Basic and Clinical Pharmacology. LXXV. Nomenclature, Classification, and Pharmacology of G Protein-Coupled Melatonin Receptors (2010, background): “These residues form hydrogen bonds to the peptide backbone and thereby bend and twist helices (Gray and Matthews, 1984; Ballesteros et al., 2000).”