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PMID: 10805128 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings.

Journal of biomolecular NMR ·Vol. 16 ·No. 3 ·2000-03-00 ·Pages 221-7

Permi P, Annila A

Abstract

Three transverse relaxation optimised NMR experiments (TROSY) for the measurement of scalar and dipolar couplings suitable for proteins dissolved in aqueous iso- and anisotropic solutions are described. The triple-spin-state-selective experiments yield couplings between 1HN-13Calpha, 15N-13Calpha, 1HN-13Calpha(i-1), 15N-13Calpha(i-1), 1HN-13C'(i-1), 15N-13C'(i-1) and 13C'(i-1)-13Calpha(i-1) without introducing nonessential spectral crowding compared with an ordinary two-dimensional 15N-1H correlation spectrum and without requiring explicit knowledge of carbon assignments. This set of alpha/beta-J-TROSY experiments is most useful for perdeuterated proteins in studies of structure-activity relationships by NMR to observe, in addition to epitopes for ligands, also conformational changes induced by binding of ligands.

MeSH Terms
Carbon Isotopes Hydrogen Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular Proteins/chemistry Solutions
Chemicals
Carbon Isotopes Nitrogen Isotopes Proteins Solutions Hydrogen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Permi P
Institute of Biotechnology, NMR Laboratory, University of Helsinki, Finland.
Annila A
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28 references, click to expand
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Article Info
Journal
Journal of biomolecular NMR
Abbr.
J Biomol NMR
ISSN
0925-2738
DOI
10.1023/a:1008362211560
Published
2000-03-00
Pages
221-7
Language
English
Region
Netherlands
NLM ID
9110829
Subset
IM
External Links
PubMed source DOI: 10.1023/a:1008362211560 View journal details
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