Conformations of the glycine dipeptide

Wan F. Lau; B. Montgomery Pettitt

doi:10.1002/bip.360261102

Conformations of the glycine dipeptide

Wan F. Lau, B. Montgomery Pettitt

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

Integral equation theory is applied to the determination of the intramolecular potential of mean force for the glycine dipeptide, N‐acetyl glycyl‐N‐methylamide, in aqueous solution. The solvated free energy for the dipeptide as a function of the dihedral angles ϕ and ψ (Ramachandran plot) is determined and compared with the vacuum surface. Conformations forbidden in vacuum are found to be populated in aqueous solution. The results of the glycine dipeptide are compared to a parallel study on the alanine dipeptide. Solvent effects are found to be responsible for the extent of many of glycines properties related to flexibility.

Original language	English (US)
Pages (from-to)	1817-1831
Number of pages	15
Journal	Biopolymers
Volume	26
Issue number	11
DOIs	https://doi.org/10.1002/bip.360261102
State	Published - Nov 1987
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Biomaterials
Organic Chemistry

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author = "Lau, {Wan F.} and {Montgomery Pettitt}, B.",

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AB - Integral equation theory is applied to the determination of the intramolecular potential of mean force for the glycine dipeptide, N‐acetyl glycyl‐N‐methylamide, in aqueous solution. The solvated free energy for the dipeptide as a function of the dihedral angles ϕ and ψ (Ramachandran plot) is determined and compared with the vacuum surface. Conformations forbidden in vacuum are found to be populated in aqueous solution. The results of the glycine dipeptide are compared to a parallel study on the alanine dipeptide. Solvent effects are found to be responsible for the extent of many of glycines properties related to flexibility.

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Conformations of the glycine dipeptide

Abstract

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