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 Theoretical conformational analysis was carried out for Ac-(Val-Pro-Gly-Gly) 6-NHMe with cis peptide bond at Val-Pro portion. A right-handed β 11.6-helix was found as the lowest-energy helical conformation for this polypeptide with cis peptide bond. The energy difference between β 11.6-helix and γ-helix, which is the lowest-energy helical conformation with trans peptide bond, is 3.08 kcal/mol per repeating unit(Val-Pro-Gly-Gly sequence). This value almost corresponds to the energy difference between the most stable cis and trans conformations of Ac-Val-Pro-Gly-Gly-NHMe (2.75 kcal/mol). Obtained results indicate that γ-helix is the most stable helical conformation of poly(Val-Pro-Gly-Gly) which is a model polypeptide of elastin, and also that relative stabilities of trans and cis conformations of polypeptide are essentially estimated by short-range interactions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00338904
