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Predictions of protein backbone bond distances and angles from first principles
Author(s) -
Scháfer Lothar,
Cao Ming,
Meadows Mary Jane
Publication year - 1995
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360350606
Subject(s) - chemistry , ab initio , resolution (logic) , crystallography , bond length , molecular geometry , peptide bond , low resolution , peptide , protein structure , high resolution , representation (politics) , protein structure prediction , geometry , molecule , crystal structure , mathematics , artificial intelligence , biochemistry , remote sensing , organic chemistry , politics , computer science , political science , law , geology
A procedure is described, based on a spline‐function representation of ab initio peptide conformational geometry maps, that allows one to predict backbone bond distances and angles of proteins as functions of the peptide ϕ(N‐C α )/Ψ(C α ‐C′) torsions with an accuracy comparable to that of high‐resolution protein crystallography. For example, for the more than 40 residues of crambin, the rms deviation between predicted and crystallographic values of N‐C α ‐C′ is 1.9° for the 1.5 Å resolution structure and 1.9° for the 0.83 Å resolution structure, compared with angle variations of < 10°. Accurate information on protein backbone geometries is important for establishing dictionaries of flexible geometry functions for use in empirical peptide and protein modeling. © 1995 John Wiley & Sons, Inc.