liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively C-13 labeled samples
University of Toronto, Departments of Biochemistry, Chemistry and Medical Genetics.
University of Toronto, Departments of Biochemistry, Chemistry and Medical Genetics.
University of Toronto, Departments of Biochemistry, Chemistry and Medical Genetics.
2008 (English)In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 42, no 1, 35-47 p.Article in journal (Refereed) Published
Abstract [en]

Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion nuclear magnetic resonance (NMR) spectroscopy has emerged as a powerful method for quantifying chemical shifts of excited protein states. For many applications of the technique that involve the measurement of relaxation rates of carbon magnetization it is necessary to prepare samples with isolated C-13 spins so that experiments do not suffer from magnetization transfer between coupled carbon spins that would otherwise occur during the CPMG pulse train. In the case of (CO)-C-13 experiments however the large separation between (CO)-C-13 and C-13(alpha) chemical shifts offers hope that robust (CO)-C-13 dispersion profiles can be recorded on uniformly C-13 labeled samples, leading to the extraction of accurate (CO)-C-13 chemical shifts of the invisible, excited state. Here we compare such chemical shifts recorded on samples that are selectively labeled, prepared using [1-C-13]-pyruvate and (NaHCO3,)-C-13 or uniformly labeled, generated from C-13-glucose. Very similar (CO)-C-13 chemical shifts are obtained from analysis of CPMG experiments recorded on both samples, and comparison with chemical shifts measured using a second approach establishes that the shifts measured from relaxation dispersion are very accurate.

Place, publisher, year, edition, pages
2008. Vol. 42, no 1, 35-47 p.
Keyword [en]
ISOTOPICALLY ENRICHED PROTEINS; SECONDARY STRUCTURE; SH3 DOMAIN; RESOLUTION ENHANCEMENT; C-13-ENRICHED PROTEINS; SEQUENCE HOMOLOGY; DIPOLAR COUPLINGS; SPIN RELAXATION; METHYL-GROUPS; C-ALPHA
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:liu:diva-51909DOI: 10.1007/s10858-008-9260-4OAI: oai:DiVA.org:liu-51909DiVA: diva2:278094
Available from: 2009-11-23 Created: 2009-11-23 Last updated: 2017-12-12

Open Access in DiVA

No full text

Other links

Publisher's full text

Authority records BETA

Lundström, Patrik

Search in DiVA

By author/editor
Lundström, Patrik
In the same journal
Journal of Biomolecular NMR
Structural Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 53 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf