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- W2034982660 endingPage "635" @default.
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- W2034982660 abstract "The conformational characteristics of the peptide sequence X-l-Pro, where X Gly or l-Ala and the peptide bond joining X and l-Pro is cis, are evaluated. Semi-empirical potential functions are used to estimate the contributions to the conformational energy made by the non-bonded van der Waals' and electrostatic interactions and the intrinsic torsional potentials about the NCa and CaC′ bonds. Rotations φ1 and ψ1 about the NCa and CaC′ bonds in residue X and rotation ψ2 about the CaC′ bond in l-Pro are permitted, while the angle of rotation φ2 about the NCa bond in l-Pro is fixed at 120 ° by the pyrrolidine ring. The presence of the cis peptide bond connecting X and l-Pro renders the backbone rotations φ1, ψ1 in X dependent upon the rotation ψ2 about the CaC′ bond in l-Pro. (Interdependence of rotations in neighboring residues joined by a cis peptide bond was previously observed in l-alanine oligomers.) The number of energetically allowed conformations for the Gly and l-Ala residues preceding a cis peptide bond l-Pro residue are found to be substantially reduced from those permitted when the peptide bond is trans or when l-Pro is replaced by an amino acid residue. On the other hand, ψ2 = 100 to 160 ° (cis′) and 300 to 0 ° (trans′) are found to be the lowest energy conformations of the l-Pro residue irrespective of the cis or trans conformation of the X-l-Pro peptide bond." @default.
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- W2034982660 date "1974-07-01" @default.
- W2034982660 modified "2023-10-16" @default.
- W2034982660 title "Conformational characteristics of polypeptides containing isolated l-Proline residues with cis peptide bonds" @default.
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- W2034982660 doi "https://doi.org/10.1016/0022-2836(74)90185-5" @default.
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