Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [15N,1H]-TROSY-HNC experiment

Wienk, Hans L.J., Martinez, Mitcheell M., Yalloway, Gary N., Schmidt, Jürgen M., Perez, Carlos S, Rüterjans, Heinz, Löhr, Frank (2003) Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [15N,1H]-TROSY-HNC experiment. Journal of Biomolecular NMR, 25 (2). pp. 133-145. ISSN 0925-2738 (Print) 1573-5001 (Online). (doi:10.1023/A:1022233103990) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:22839)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL: http://dx.doi.org/10.1023/A:1022233103990

Abstract

A quantitative J-correlation pulse sequence is described that allows simultaneous determination of one-bond and two-bond nitrogen-carbon coupling constants for protonated or deuterated proteins. Coupling constants are calculated from volume ratios between cross peaks and reference axial peaks observed in a single 3D spectrum. Accurate backbone 1JNC', 1JNC?, and 2JNC? coupling constants are obtained for the two [15N;13C]-labeled, medium-sized proteins flavodoxin and xylanase and for the [2H;15N;13C]-labeled, large protein DFPase. A dependence of onebond and two-bond JNC? values on protein backbone ? torsion angles is readily apparent, in agreement with previously found correlations. In addition, the experiment is performed on isotropic as well as aligned protein to measure associated 15N-13C residual dipolar couplings.

Item Type:	Article
DOI/Identification number:	10.1023/A:1022233103990
Uncontrolled keywords:	DFPase, flavodoxin, perdeuteration, residual dipolar coupling, scalar coupling, TROSY, xylanase
Subjects:	Q Science Q Science > QD Chemistry Q Science > QP Physiology (Living systems) Q Science > QC Physics Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions:	Divisions > Division of Natural Sciences > Biosciences
Depositing User:	Jurgen M Schmidt
Date Deposited:	30 Sep 2009 15:56 UTC
Last Modified:	16 Nov 2021 10:01 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/22839 (The current URI for this page, for reference purposes)

University of Kent Author Information

Schmidt, Jürgen M..

Creator's ORCID:
CReDIT Contributor Roles:

Depositors only (login required):

Altmetric

Download Statistics

Total unique views for this document in KAR since July 2020. For more details click on the image.