Deviations from planarity of the peptide bond in peptides and proteins.
The work described here is the result of a survey of the peptide omega angles in the Cambridge Structural Database of small molecules, which was carried out to establish "ideal" or "target" values for their distribution. We have shown that substantial deviations from planarity can be tolerated with a standard deviation in the angle of up to 6 degrees about a mean value for the trans peptide that is less than 180 degrees . The distortion can arise from pyramidalization at the amino nitrogen atom as well as simple twist about the peptide bond. We include an analysis of omega angles in the existing database of protein structure (PDB) and show that their distributions can depend on the refinement method used, but no correlation with resolution is evident. A surprising finding was a systematic variation of omega in phi,psi space in proteins as well as in the linear and cyclic peptides. This is particularly manifest as a consistent difference between the mean omega values in chains of left and right-hand chirality. This dichotomy is observed for all the standard amino acids and is especially striking in the absence of secondary structure. The phenomenon is discussed in the context of theoretical work on peptide analogues, and the implications for protein conformation and structure are briefly considered.
MacArthur
M W
MW
Department of Biochemistry and Molecular Biology, University College, London, England.
Thornton
J M
JM
D000596:Amino Acids / Q000032:analysis; D018360:Crystallography, X-Ray; D016208:Databases, Factual; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D000596:Amino Acids; D010455:Peptides; D011506:Proteins