title: Alpha helix capping and the conformation of threonine.
abstract: The amino acid threonine contains two chiral carbons and thus can exist in four possible conformations. However, only a single conformation (2S, 3R) of threonine is incorporated in proteins by the cellular translation material. The conformation at the alpha carbon (carbon 2) is the same as that of the other amino acids in biological proteins, and there is no explanation for why this enantiomer was selected. Further, there is no explanation for the choice of conformation at the 3 carbon in threonine. Here, I suggest that the preferential ability of (2S, 3R) threonine over the (2S, 3S) enantiomer to participate in alpha helix capping interactions may have led to the selection of the (2S, 3R) conformation.
authors.affiliation: Brain and Reception Laboratory and Institute for Neural Computation, University of California, San Diego, La Jolla, California 92093-0109, USA. ealtschuler@ucsd.edu
authors.forename: E L
authors.initials: EL
authors.lastname: Altschuler
mesh_terms: D006860:Hydrogen Bonding; D015394:Molecular Structure; D013912:Threonine / Q000737:chemistry*
chemical_list: D013912:Threonine