[NMR paper] Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1? NMR Measurements: Application to Protein Backbone Dynamics Measurements.
Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1? NMR Measurements: Application to Protein Backbone Dynamics Measurements.
Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1? NMR Measurements: Application to Protein Backbone Dynamics Measurements.
J Phys Chem B. 2016 Aug 8;
Authors: Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P
Abstract
Transverse relaxation rate measurements in MAS solid-state NMR provide information about molecular motions occurring on nanoseconds-to-milliseconds (ns-ms) time scales. The measurement of heteronuclear (13C, 15N) relaxation rate constants in the presence of a spin-lock radio-frequency field (R1? relaxation) provides access to such motions, and an increasing number of studies involving R1? relaxation in proteins has been reported. However, two factors that influence the observed relaxation rate constants have so far been neglected, namely (i) the role of CSA/dipolar cross-correlated relaxation (CCR), and (ii) the impact of fast proton spin flips (i.e. proton spin diffusion and relaxation). We show that CSA/D CCR in R1? experiments is measurable, and that this cross-correlated relaxation rate constant depends on ns-ms motions, and can thus itself provide insight into dynamics. We find that proton spin-diffusion attenuates this cross-correlated relaxation, due to its decoupling effect on the doublet components. For measurements of dynamics, the use of R1? rate constants has practical advantages over the use of CCR rates, and the present manuscript reveals factors that have so far been disregarded and which are important for accurate measurements and interpretation.
PMID: 27500976 [PubMed - as supplied by publisher]
Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins
Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00670/20151110/images/medium/bi-2015-006703_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00670
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/ypRveS3_Ty0
More...
nmrlearner
Journal club
0
11-12-2015 09:05 AM
Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins
Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins
Abstract
Adiabatically swept pulses were originally designed for the purpose of broadband spin inversion. Later, unexpected advantages of their utilization were also found in other applications, such as refocusing to excite spin echoes, studies of chemical exchange or fragment-based drug design. Here, we present new experiments to characterize fast (psā??ns) protein dynamics, which benefit from little-known properties of adiabatic pulses. We...
nmrlearner
Journal club
0
10-28-2015 05:05 PM
[NMR paper] Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Related Articles Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Phys Chem Chem Phys. 2015 Aug 3;
Authors: Lamley JM, Lougher MJ, Sass HJ, Rogowski M, Grzesiek S, Lewandowski JR
Abstract
Typically, protein dynamics involve a complex hierarchy of motions occurring on different time scales between conformations separated by a range...
nmrlearner
Journal club
0
08-04-2015 03:00 PM
[NMR paper] A Magic-Angle Spinning NMR Method for the Site-Specific Measurement of Proton Chemical-Shift Anisotropy in Biological and Organic Solids.
A Magic-Angle Spinning NMR Method for the Site-Specific Measurement of Proton Chemical-Shift Anisotropy in Biological and Organic Solids.
Related Articles A Magic-Angle Spinning NMR Method for the Site-Specific Measurement of Proton Chemical-Shift Anisotropy in Biological and Organic Solids.
Isr J Chem. 2014 Feb 1;54(1-2):171-183
Authors: Hou G, Gupta R, Polenova T, Vega AJ
Abstract
Proton chemical shifts are a rich probe of structure and hydrogen bonding environments in organic and biological molecules. Until recently,...
nmrlearner
Journal club
0
12-09-2014 01:13 PM
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Publication date: 7 October 2014
Source:Biophysical Journal, Volume 107, Issue 7</br>
Author(s): Ryan*H. Lo , Brett*M. Kroncke , Tsega*L. Solomon , Linda Columbus</br>
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...
nmrlearner
Journal club
0
10-08-2014 04:17 AM
Multidimensional Magic Angle Spinning NMR Spectroscopy for Site-Resolved Measurement of Proton Chemical Shift Anisotropy in Biological Solids
Multidimensional Magic Angle Spinning NMR Spectroscopy for Site-Resolved Measurement of Proton Chemical Shift Anisotropy in Biological Solids
Guangjin Hou, Sivakumar Paramasivam, Si Yan, Tatyana Polenova and Alexander J. Vega
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3084972/aop/images/medium/ja-2012-084972_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3084972
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/y3Jt7S8MwHM
nmrlearner
Journal club
0
01-22-2013 09:14 PM
[NMR paper] Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Related Articles Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
J Am Chem Soc. 2005 Aug 31;127(34):11946-7
Authors: Wylie BJ, Franks WT, Graesser DT, Rienstra CM
In this Communication, we introduce a 3D magic-angle spinning recoupling experiment that correlates chemical shift...
nmrlearner
Journal club
0
12-01-2010 06:56 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...