Publication date: 7 October 2014 Source:Biophysical Journal, Volume 107, Issue 7
Author(s): Ryan*H. Lo , Brett*M. Kroncke , Tsega*L. Solomon , Linda Columbus
The ability to detect nanosecond backbone dynamics with site-directed spin labeling (SDSL) in soluble proteins has been well established. However, for membrane proteins, the nitroxide appears to have more interactions with the protein surface, potentially hindering the sensitivity to backbone motions. To determine whether membrane protein backbone dynamics could be mapped with SDSL, a nitroxide was introduced at 55 independent sites in a model polytopic membrane protein, TM0026. Electron paramagnetic resonance spectral parameters were compared with NMR 15N-relaxation data. Sequential scans revealed backbone dynamics with the same trends observed for the R1 relaxation rate, suggesting that nitroxide dynamics remain coupled to the backbone on membrane proteins.
[NMR paper] Mapping the UDP-N-acetylglucosamine regulatory site of human glucosamine-6P synthase by saturation-transfer difference NMR and site-directed mutagenesis.
Mapping the UDP-N-acetylglucosamine regulatory site of human glucosamine-6P synthase by saturation-transfer difference NMR and site-directed mutagenesis.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Mapping the UDP-N-acetylglucosamine regulatory site of human glucosamine-6P synthase by saturation-transfer difference NMR and site-directed mutagenesis.
Biochimie. 2014 Feb;97:39-48
Authors: Assrir N, Richez C, Durand P, Guittet E, Badet B, Lescop E,...
nmrlearner
Journal club
0
08-27-2014 02:29 PM
[NMR paper] Carbon Relaxation in (13)C(?)-H(?) and (13)C(?)-D(?) Spin Pairs as a Probe of Backbone Dynamics in Proteins.
Carbon Relaxation in (13)C(?)-H(?) and (13)C(?)-D(?) Spin Pairs as a Probe of Backbone Dynamics in Proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Carbon Relaxation in (13)C(?)-H(?) and (13)C(?)-D(?) Spin Pairs as a Probe of Backbone Dynamics in Proteins.
J Phys Chem B. 2013 Jan 25;
Authors: Sun H, Long D, Brüschweiler R, Tugarinov V
Abstract
NMR methodology for the measurements of ?-carbon R(1) and R(1?) spin relaxation rates in (13)C(?)-H(?) and (13)C(?)-D(?) spin...
nmrlearner
Journal club
0
02-03-2013 10:22 AM
[NMR paper] Water proton spin saturation affects measured protein backbone 15N spin relaxation rates
From Mendeley Biomolecular NMR group:
Water proton spin saturation affects measured protein backbone 15N spin relaxation rates
Journal of Magnetic Resonance (2011). Volume: 213, Issue: 1. Pages: 151-157. Kang Chen, Nico Tjandra et al.
Published using Mendeley: The digital library for researchers
nmrlearner
Journal club
0
08-24-2012 08:01 PM
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Tomasz L. Religa, Amy M. Ruschak, Rina Rosenzweig and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202259a/aop/images/medium/ja-2011-02259a_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202259a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/rQfCMlQFoW8
nmrlearner
Journal club
0
05-20-2011 09:17 PM
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
J Am Chem Soc. 2011 May 11;
Authors: Religa TL, Ruschak AM, Rosenzweig R, Kay LE
Methyl groups are powerful reporters of structure, motion and function in NMR studies of supra-molecular protein assemblies. Their...
nmrlearner
Journal club
0
05-12-2011 03:40 PM
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Angew Chem Int Ed Engl. 2011 Mar 18;
Authors: Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M
nmrlearner
Journal club
0
03-23-2011 05:41 PM
[NMR paper] Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements.
Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements.
Related Articles Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements.
Biochemistry. 2005 Jul 19;44(28):9673-9
Authors: Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL
Nuclear magnetic resonance (NMR) (15)N relaxation measurements of the olfactory marker protein (OMP) including longitudinal relaxation (T(1)), transverse relaxation (T(2)), and (15)N-{(1)H} NOE data were collected at low...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] A comparison of 15N NMR relaxation measurements with a molecular dynamics simulation:
A comparison of 15N NMR relaxation measurements with a molecular dynamics simulation: backbone dynamics of the glucocorticoid receptor DNA-binding domain.
Related Articles A comparison of 15N NMR relaxation measurements with a molecular dynamics simulation: backbone dynamics of the glucocorticoid receptor DNA-binding domain.
Proteins. 1993 Dec;17(4):375-90
Authors: Eriksson MA, Berglund H, Härd T, Nilsson L
The rapid motions of the backbone of the DNA-binding domain of the glucocorticoid receptor (GR DBD) have been investigated using...
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Linear Mode
