PMID: 708779Oct 23, 1978Paper

Proton magnetic resonance and conformational energy calculations of repeat peptides of tropoelastin. A permutation of the hexapeptide

Biochimica Et Biophysica Acta
V RenugopalakrishnanD W Urry

Abstract

The conformation of a hexapeptide sequence occurring in tropoelastin is discussed from the results obtained using a combined approach of theoretical conformational energy calculations on HCO-Val-Ala-Prb-Gly-OMe and 1h nmr studies on t-Boc-Val-Ala-Pro-Gly-Val-Gly-OMe in a dilute solution of methanol. Both studies have reasonable concurrence with respect to the preferred conformation of the hexapeptide and an analysis of the combined results suggests that the hexapeptide is stabilized by a beta-turn involving the Ala1,iC=O and Val4,iNH groups and a gamma-turn involving Gly5,iC=O and Gly3,iNH groups. A weaker interaction between Gly3,iC=O and Gly5,iNH groups is also found to be possible. Conformational features of the first valyl residue in the sequence Val-Ala-Pro-Gly-Val-Gly and the last valyl residue in Ala-Pro-Gly-Val-Gly-Val are compared and found to have similar torsion angles. The implications of such a similarity are discussed with respect to the conformation of the polyhexapeptide.

Citations

Jan 1, 1980·CRC Critical Reviews in Biochemistry·J A Smith, L G Pease
Jul 10, 2019·Matrix Biology : Journal of the International Society for Matrix Biology·Arturo Ibáñez-FonsecaJosé Carlos Rodríguez-Cabello

Related Concepts

Kappa-Elastin
In Vivo NMR Spectroscopy
Peptide Fragments
Protein Conformation
Protein Precursors
Thermodynamics

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