Enhanced stability of cis Pro-Pro peptide bond in Pro-Pro-Phe sequence motif.
Identification of sequence motifs that favor cis peptide bonds in proteins is important for understanding and designing proteins containing turns mediated by cis peptide conformations. From (1)H NMR solution studies on short peptides, we show that the Pro-Pro peptide bond in Pro-Pro-Phe almost equally populates the cis and trans isomers, with the cis isomer stabilized by a CHc...pi interaction involving the terminal Pro and Phe. We also show that Phe is over-represented at sequence positions immediately following cis Pro-Pro motifs in known protein structures. Our results demonstrate that the Pro-Pro cis conformer in Pro-Pro-Phe sequence motifs is as important as the trans conformer, both in short peptides as well as in natively folded proteins.
Dasgupta
Bhaskar
B
Department of Biochemistry, Bose Institute, P-1/12 CIT, Scheme VIIM, Kolkata 700 054, India.
Chakrabarti
Pinak
P
Basu
Gautam
G
D000595:Amino Acid Sequence; D003903:Deuterium / Q000737:chemistry; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D011485:Protein Binding; D013237:Stereoisomerism
D009842:Oligopeptides; D010649:Phenylalanine; D011392:Proline; D003903:Deuterium