title: Glycine rescue of β-sheets from cis-proline.
abstract: Proline is incompatible with ideal β-sheet geometry, and the incompatibility gets magnified when Pro assumes the cis peptidyl-prolyl conformation. We show that Gly appears with high propensity at pre-cisPro positions in β-sheets and rescues the β-sheet from severe distortions by assuming a right-handed polyproline conformation (β(PR)), effectively increasing the local β-sheet register by one residue. The united residue, Gly(β(PR))-cisPro, is evolutionarily conserved, functionally important, and dynamic in nature.
authors.affiliation: Bioinformatics Centre, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700054, India.
authors.forename: Madhurima
authors.initials: M
authors.lastname: Das
authors.forename: Gautam
authors.initials: G
authors.lastname: Basu
mesh_terms: D000595:Amino Acid Sequence; D005998:Glycine / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D010455:Peptides; D011506:Proteins; C011083:polyproline; D011392:Proline; D005998:Glycine