[NMR paper] Probing Side-Chain Dynamics in Proteins by NMR Relaxation of Isolated (13)C Magnetization Modes in (13)CH(3) Methyl Groups
Probing Side-Chain Dynamics in Proteins by NMR Relaxation of Isolated (13)C Magnetization Modes in (13)CH(3) Methyl Groups
The dynamics of methyl-bearing side chains in proteins were probed by ^(13)C relaxation measurements of a number of ^(13)C magnetization modes in selectively ^(13)CH(3)-labeled methyl groups of proteins. We first show how ^(13)C magnetization modes in a ^(13)CH(3) spin-system can be isolated using acute-angle ¹H radio-frequency pulses. The parameters of methyl-axis dynamics, a measure of methyl-axis ordering (S(axis)²) and the correlation time of fast local methyl-axis...
NMR relaxation parameters of methyl groups as a tool to map the interfaces of helixâ??helix interactions in membrane proteins
NMR relaxation parameters of methyl groups as a tool to map the interfaces of helixâ??helix interactions in membrane proteins
Abstract
In the case of soluble proteins, chemical shift mapping is used to identify the intermolecular interfaces when the NOE-based calculations of spatial structure of the molecular assembly are impossible or impracticable. However, the reliability of the membrane protein interface mapping based on chemical shifts or other relevant parameters was never assessed. In the present work, we investigate the predictive power of...
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10-24-2017 05:09 PM
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Xiaolin Xu, Andrey V. Struts, Aswini Kumar Giri, Trivikram R. Molugu, Charitha Guruge, Samira Faylough, Carolina L. Nascimento, Nasri Nesnas, Victor J. Hruby, Michael F. Brown</br>
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02-17-2016 07:50 PM
Measurement of 15N relaxation rates in perdeuterated proteins by TROSY-based methods
Measurement of 15N relaxation rates in perdeuterated proteins by TROSY-based methods
<div class="Abstract" lang="en">Abstract <div class="normal">While extracting dynamics parameters from backbone 15N relaxation measurements in proteins has become routine over the past two decades, it is increasingly recognized that accurate quantitative analysis can remain limited by the potential presence of systematic errors associated with the measurement of 15N R1 and R2 or R1Ï? relaxation rates as well as heteronuclear 15N-{1H} NOE values. We show that systematic errors in such measurements can...
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06-16-2012 06:01 AM
Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in [13CH3]-Methyl-Labeled, Deuterated Proteins
Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in -Methyl-Labeled, Deuterated Proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Hechao Sun, Vitali Tugarinov</br>
A pair of NMR experiments is developed for separation of individual fast-relaxing transitions in 13CH3 methyl groups of methyl-protonated, highly deuterated proteins, and the measurement of their relaxation rates. Intra-methyl 1H-1H/1H-13C dipole-dipole cross-correlated spin relaxation that differentiates the rates of the fast-relaxing transitions...
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03-09-2012 09:16 AM
Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in [CH3]-Methyl-Labeled, Deuterated Proteins
Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in -Methyl-Labeled, Deuterated Proteins
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 2 March 2012</br>
Hechao*Sun, Vitali*Tugarinov</br>
A pair of NMR experiments is developed for separation of individual fast-relaxing transitions inCH3methyl groups of methyl-protonated, highly deuterated proteins, and the measurement of their relaxation rates. Intra-methylH-H/H-C dipole-dipole cross-correlated spin relaxation that differentiates the rates of the fast-relaxing...
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03-06-2012 06:04 AM
Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange
Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange
Abstract Although originally designed for broadband inversion and decoupling in NMR spectroscopy, recent methodological developments have introduced adiabatic fast passage (AFP) pulses into the field of protein dynamics. AFP pulses employ a frequency sweep, and have not only superior inversion properties with respect to offset effects, but they are also easily implemented into a pulse sequence. As magnetization is dragged from the +z to...
The Measurement of Relaxation Rates of Degenerate 1H Transitions in Methyl Groups of Proteins Using Acute Angle Radiofrequency Pulses
Linear Mode
