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

Direct link
Measuring the Signs of H-1(alpha) Chemical Shift Differences Between Ground and Excited Protein States by Off-Resonance Spin-Lock R-1 rho NMR Spectroscopy
University of Toronto.
University of Toronto.
University of Toronto.
Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology . Linköping University, The Institute of Technology.
Show others and affiliations
2009 (English)In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, ISSN 0002-7863, Vol. 131, no 31, 10832-10833 p.Article in journal (Refereed) Published
Abstract [en]

Analysis of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR profiles provides the kinetics and thermodynamics of millisecond-time-scale exchange processes involving the interconversion of populated ground and invisible excited states. In addition, the absolute values of chemical, shift differences between NMR probes in the exchanging states, vertical bar Delta(pi)vertical bar, are also extracted. Herein, we present a simple experiment for obtaining the sign of H-1(alpha) Delta(pi) values by measuring off-resonance H-1(alpha) decay rates, R-1 rho, using weak proton spin-lock fields. A pair of R-1 rho values is measured with a spin-lock field applied vertical bar Delta omega vertical bar downfield and upfield of the major-state peak. In many cases, these two relaxation rates differ substantially, with the larger one corresponding to the case where the spin-lock field coincides with the resonance frequency of the probe in the minor state. The utility of the methodology is demonstrated first on a system involving protein ligand exchange and subsequently on an SH3 domain exchanging between a folded state and its on-pathway folding intermediate. With this experiment, it thus becomes possible to determine H-1(alpha) chemical shifts of the invisible excited state, which can be used as powerful restraints in defining the structural properties of these elusive conformers.

Place, publisher, year, edition, pages
2009. Vol. 131, no 31, 10832-10833 p.
National Category
Natural Sciences
URN: urn:nbn:se:liu:diva-19998DOI: 10.1021/ja904315mOAI: diva2:232453
Available from: 2009-08-24 Created: 2009-08-24 Last updated: 2009-08-24

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Lundström, Patrik
By organisation
Molecular Biotechnology The Institute of Technology
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 26 hits
ReferencesLink to record
Permanent link

Direct link