Peptide models XXXI. Conformational properties of hydrophobic residues shaping the core of proteins. An ab initio study of n-formyl-L-valinamide and n-formyl-L-phenylalaninamide

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Employing introductory (3-21G RHF) and medium-size (6-311++G**B3LYP) ab initio calculations, complete conformational libraries, containing as many as 27 conformers, have been determined for diamide model systems incorporating the amino acids valine (Val) and phenylalanine (Phe). Conformational and energetic properties of these libraries were analyzed. For example, significant correlation was found between relative energies from 6-311++G** B3LYP and single-point B3LYP/6-311++G**//RHF/3-21G calculations. Comparison of populations of molecular conformations of hydrophobic aromatic and nonaromatic residues, based on their ab initio relative energies, with their natural abundance indicates that, at least for the hydrophobic core of proteins, the conformations of Val (Ile, Leu) and Phe (Tyr, Trp) are controlled by the local energetic preferences of the respective amino acids.

Original languageEnglish
Pages (from-to)732-751
Number of pages20
JournalJournal of Computational Chemistry
Volume22
Issue number7
DOIs
Publication statusPublished - May 2001

Fingerprint

Valine
Phenylalanine
Peptides
Conformations
Amino Acids
Amino acids
Molecular Conformation
Diamide
Proteins
Protein
Ab Initio Calculations
Energy
Conformation
Model
Libraries

Keywords

  • Ab initio calculations
  • Hydrophobic residues
  • Peptides and proteins

ASJC Scopus subject areas

  • Chemistry(all)
  • Safety, Risk, Reliability and Quality

Cite this

@article{9d753b8f826145dab612d6d247cc6d0b,
title = "Peptide models XXXI. Conformational properties of hydrophobic residues shaping the core of proteins. An ab initio study of n-formyl-L-valinamide and n-formyl-L-phenylalaninamide",
abstract = "Employing introductory (3-21G RHF) and medium-size (6-311++G**B3LYP) ab initio calculations, complete conformational libraries, containing as many as 27 conformers, have been determined for diamide model systems incorporating the amino acids valine (Val) and phenylalanine (Phe). Conformational and energetic properties of these libraries were analyzed. For example, significant correlation was found between relative energies from 6-311++G** B3LYP and single-point B3LYP/6-311++G**//RHF/3-21G calculations. Comparison of populations of molecular conformations of hydrophobic aromatic and nonaromatic residues, based on their ab initio relative energies, with their natural abundance indicates that, at least for the hydrophobic core of proteins, the conformations of Val (Ile, Leu) and Phe (Tyr, Trp) are controlled by the local energetic preferences of the respective amino acids.",
keywords = "Ab initio calculations, Hydrophobic residues, Peptides and proteins",
author = "A. Perczel",
year = "2001",
month = "5",
doi = "10.1002/jcc.1040",
language = "English",
volume = "22",
pages = "732--751",
journal = "Journal of Computational Chemistry",
issn = "0192-8651",
publisher = "John Wiley and Sons Inc.",
number = "7",

}

TY - JOUR

T1 - Peptide models XXXI. Conformational properties of hydrophobic residues shaping the core of proteins. An ab initio study of n-formyl-L-valinamide and n-formyl-L-phenylalaninamide

AU - Perczel, A.

PY - 2001/5

Y1 - 2001/5

N2 - Employing introductory (3-21G RHF) and medium-size (6-311++G**B3LYP) ab initio calculations, complete conformational libraries, containing as many as 27 conformers, have been determined for diamide model systems incorporating the amino acids valine (Val) and phenylalanine (Phe). Conformational and energetic properties of these libraries were analyzed. For example, significant correlation was found between relative energies from 6-311++G** B3LYP and single-point B3LYP/6-311++G**//RHF/3-21G calculations. Comparison of populations of molecular conformations of hydrophobic aromatic and nonaromatic residues, based on their ab initio relative energies, with their natural abundance indicates that, at least for the hydrophobic core of proteins, the conformations of Val (Ile, Leu) and Phe (Tyr, Trp) are controlled by the local energetic preferences of the respective amino acids.

AB - Employing introductory (3-21G RHF) and medium-size (6-311++G**B3LYP) ab initio calculations, complete conformational libraries, containing as many as 27 conformers, have been determined for diamide model systems incorporating the amino acids valine (Val) and phenylalanine (Phe). Conformational and energetic properties of these libraries were analyzed. For example, significant correlation was found between relative energies from 6-311++G** B3LYP and single-point B3LYP/6-311++G**//RHF/3-21G calculations. Comparison of populations of molecular conformations of hydrophobic aromatic and nonaromatic residues, based on their ab initio relative energies, with their natural abundance indicates that, at least for the hydrophobic core of proteins, the conformations of Val (Ile, Leu) and Phe (Tyr, Trp) are controlled by the local energetic preferences of the respective amino acids.

KW - Ab initio calculations

KW - Hydrophobic residues

KW - Peptides and proteins

UR - http://www.scopus.com/inward/record.url?scp=20644432852&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=20644432852&partnerID=8YFLogxK

U2 - 10.1002/jcc.1040

DO - 10.1002/jcc.1040

M3 - Article

AN - SCOPUS:20644432852

VL - 22

SP - 732

EP - 751

JO - Journal of Computational Chemistry

JF - Journal of Computational Chemistry

SN - 0192-8651

IS - 7

ER -