Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins

J. Howard Bradbury, Raymond S. Norton

Research output: Contribution to journalArticleResearchpeer-review

36 Citations (Scopus)

Abstract

The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine · HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms.

Original languageEnglish
Pages (from-to)10-19
Number of pages10
JournalBBA - Protein Structure
Volume328
Issue number1
DOIs
Publication statusPublished - 11 Nov 1973
Externally publishedYes

Cite this

@article{84aa55c2d94642ee80ae36362a37de9d,
title = "Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins",
abstract = "The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine · HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms.",
author = "Bradbury, {J. Howard} and Norton, {Raymond S.}",
year = "1973",
month = "11",
day = "11",
doi = "10.1016/0005-2795(73)90324-3",
language = "English",
volume = "328",
pages = "10--19",
journal = "BBA - Protein Structure",
issn = "0005-2795",
number = "1",

}

Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins. / Bradbury, J. Howard; Norton, Raymond S.

In: BBA - Protein Structure, Vol. 328, No. 1, 11.11.1973, p. 10-19.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins

AU - Bradbury, J. Howard

AU - Norton, Raymond S.

PY - 1973/11/11

Y1 - 1973/11/11

N2 - The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine · HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms.

AB - The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine · HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms.

UR - http://www.scopus.com/inward/record.url?scp=0015807078&partnerID=8YFLogxK

U2 - 10.1016/0005-2795(73)90324-3

DO - 10.1016/0005-2795(73)90324-3

M3 - Article

VL - 328

SP - 10

EP - 19

JO - BBA - Protein Structure

JF - BBA - Protein Structure

SN - 0005-2795

IS - 1

ER -