Journal article
β‐Bend conformation of CH3CO‐Pro‐Pro‐Gly‐Pro‐NHCH3: Implications for posttranslational proline hydroxylation in collagen
Abstract
Abstract Conformational‐energy computations have been carried out for the N ‐acetyl‐ N ′‐methylamides of the Pro‐Pro, Pro‐Gly, and Gly‐Pro dipeptides and of the Pro‐Pro‐Gly‐Pro tetrapeptide, serving as models for the conformational analysis of single‐stranded poly(Gly‐Pro‐Pro). The probability of β‐bend formation for the Pro‐Gly sequence is very high, viz., 0.72 for the terminally blocked Pro‐Gly dipeptide, and rises to 0.86 in the …
Authors
Lee E; Némethy G; Scheraga HA; Ananthanarayanan VS
Journal
Biopolymers, Vol. 23, No. 7, pp. 1193–1206
Publisher
Wiley
Publication Date
7 1984
DOI
10.1002/bip.360230705
ISSN
0006-3525