ISSN:
1436-2449
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
,
Physics
Notes:
Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01032668
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