Conformational analysis of four β‐methylphenylalanine stereoisomers in a bioactive peptide by z‐filtered relay NMR spectroscopy

Katalin E. Kövér, Ding Jiao, Sunan Fang, Victor J Hruby

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The rotamer populations around the C‐α—C‐β bond of amino acid residues with one β‐proton can be calculated from homonuclear and heteronuclear vicinal coupling constants. The measurement of long‐range heteronuclear coupling constants, however, suffers from the inherent low sensitivity of the heteronuclear multiple bond experiments. In this paper it is demonstrated that z‐filtered homonuclear and heteronuclear relay spectroscopy provides a sensitive and accurate means for the evaluation of conformationally important vicinal coupling constants. Side‐chain conformations of the four stereoisomers of β‐methylphenylalanine residues in synthetic octapeptide analogues of CCK‐8 were derived from the measured coupling constants. This information is not easily available from conformational analysis based on simple steric considerations.

Original languageEnglish (US)
Pages (from-to)1072-1076
Number of pages5
JournalMagnetic Resonance in Chemistry
Volume31
Issue number12
DOIs
StatePublished - 1993

Fingerprint

Stereoisomerism
Peptides
Nuclear magnetic resonance spectroscopy
Conformations
Protons
Amino acids
Spectroscopy
Amino Acids
Experiments

Keywords

  • C NMR
  • H NMR
  • Conformational analysis
  • Homo‐ and heteronuclear vicinal coupling constants
  • Side‐chain conformation
  • z‐Filtered relay spectroscopy

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)

Cite this

Conformational analysis of four β‐methylphenylalanine stereoisomers in a bioactive peptide by z‐filtered relay NMR spectroscopy. / Kövér, Katalin E.; Jiao, Ding; Fang, Sunan; Hruby, Victor J.

In: Magnetic Resonance in Chemistry, Vol. 31, No. 12, 1993, p. 1072-1076.

Research output: Contribution to journalArticle

@article{1721513f2f9b42a8bdea442cd0e0d7c6,
title = "Conformational analysis of four β‐methylphenylalanine stereoisomers in a bioactive peptide by z‐filtered relay NMR spectroscopy",
abstract = "The rotamer populations around the C‐α—C‐β bond of amino acid residues with one β‐proton can be calculated from homonuclear and heteronuclear vicinal coupling constants. The measurement of long‐range heteronuclear coupling constants, however, suffers from the inherent low sensitivity of the heteronuclear multiple bond experiments. In this paper it is demonstrated that z‐filtered homonuclear and heteronuclear relay spectroscopy provides a sensitive and accurate means for the evaluation of conformationally important vicinal coupling constants. Side‐chain conformations of the four stereoisomers of β‐methylphenylalanine residues in synthetic octapeptide analogues of CCK‐8 were derived from the measured coupling constants. This information is not easily available from conformational analysis based on simple steric considerations.",
keywords = "C NMR, H NMR, Conformational analysis, Homo‐ and heteronuclear vicinal coupling constants, Side‐chain conformation, z‐Filtered relay spectroscopy",
author = "K{\"o}v{\'e}r, {Katalin E.} and Ding Jiao and Sunan Fang and Hruby, {Victor J}",
year = "1993",
doi = "10.1002/mrc.1260311208",
language = "English (US)",
volume = "31",
pages = "1072--1076",
journal = "Magnetic Resonance in Chemistry",
issn = "0749-1581",
publisher = "John Wiley and Sons Ltd",
number = "12",

}

TY - JOUR

T1 - Conformational analysis of four β‐methylphenylalanine stereoisomers in a bioactive peptide by z‐filtered relay NMR spectroscopy

AU - Kövér, Katalin E.

AU - Jiao, Ding

AU - Fang, Sunan

AU - Hruby, Victor J

PY - 1993

Y1 - 1993

N2 - The rotamer populations around the C‐α—C‐β bond of amino acid residues with one β‐proton can be calculated from homonuclear and heteronuclear vicinal coupling constants. The measurement of long‐range heteronuclear coupling constants, however, suffers from the inherent low sensitivity of the heteronuclear multiple bond experiments. In this paper it is demonstrated that z‐filtered homonuclear and heteronuclear relay spectroscopy provides a sensitive and accurate means for the evaluation of conformationally important vicinal coupling constants. Side‐chain conformations of the four stereoisomers of β‐methylphenylalanine residues in synthetic octapeptide analogues of CCK‐8 were derived from the measured coupling constants. This information is not easily available from conformational analysis based on simple steric considerations.

AB - The rotamer populations around the C‐α—C‐β bond of amino acid residues with one β‐proton can be calculated from homonuclear and heteronuclear vicinal coupling constants. The measurement of long‐range heteronuclear coupling constants, however, suffers from the inherent low sensitivity of the heteronuclear multiple bond experiments. In this paper it is demonstrated that z‐filtered homonuclear and heteronuclear relay spectroscopy provides a sensitive and accurate means for the evaluation of conformationally important vicinal coupling constants. Side‐chain conformations of the four stereoisomers of β‐methylphenylalanine residues in synthetic octapeptide analogues of CCK‐8 were derived from the measured coupling constants. This information is not easily available from conformational analysis based on simple steric considerations.

KW - C NMR

KW - H NMR

KW - Conformational analysis

KW - Homo‐ and heteronuclear vicinal coupling constants

KW - Side‐chain conformation

KW - z‐Filtered relay spectroscopy

UR - http://www.scopus.com/inward/record.url?scp=0001534216&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0001534216&partnerID=8YFLogxK

U2 - 10.1002/mrc.1260311208

DO - 10.1002/mrc.1260311208

M3 - Article

VL - 31

SP - 1072

EP - 1076

JO - Magnetic Resonance in Chemistry

JF - Magnetic Resonance in Chemistry

SN - 0749-1581

IS - 12

ER -