Conformations of the glycine dipeptide

Wan F. Lau, Bernard Pettitt

Research output: Contribution to journalArticle

30 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1817-1831
Number of pages15
JournalBiopolymers
Volume26
Issue number11
DOIs
StatePublished - 1987
Externally publishedYes

Fingerprint

Dipeptides
Glycine
Conformations
Amino acids
Vacuum
Dihedral angle
Alanine
Free energy
Integral equations

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Conformations of the glycine dipeptide. / Lau, Wan F.; Pettitt, Bernard.

In: Biopolymers, Vol. 26, No. 11, 1987, p. 1817-1831.

Research output: Contribution to journalArticle

Lau, Wan F. ; Pettitt, Bernard. / Conformations of the glycine dipeptide. In: Biopolymers. 1987 ; Vol. 26, No. 11. pp. 1817-1831.
@article{c65468e494a449b19b6fae69247625c9,
title = "Conformations of the glycine dipeptide",
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.",
author = "Lau, {Wan F.} and Bernard Pettitt",
year = "1987",
doi = "10.1002/bip.360261102",
language = "English (US)",
volume = "26",
pages = "1817--1831",
journal = "Biopolymers",
issn = "0006-3525",
publisher = "John Wiley and Sons Inc.",
number = "11",

}

TY - JOUR

T1 - Conformations of the glycine dipeptide

AU - Lau, Wan F.

AU - Pettitt, Bernard

PY - 1987

Y1 - 1987

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=84996111077&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84996111077&partnerID=8YFLogxK

U2 - 10.1002/bip.360261102

DO - 10.1002/bip.360261102

M3 - Article

VL - 26

SP - 1817

EP - 1831

JO - Biopolymers

JF - Biopolymers

SN - 0006-3525

IS - 11

ER -