Protein methyl groups can participate in multiple motional modes on different time scales. Sub-nanosecond to nano-second time scale motions of methyl axes are particularly challenging to detect for small proteins in solutions. In this work we employ NMR relaxation interference between the methyl H-H/H-C dipole-dipole interactions [Sun&Tugarinov, J. Magn. Reason. 2012] to characterize methyl axes motions as a function of temperature in a small model protein villin headpiece subdomain (HP36), in...
[NMR paper] Probing Methyl Group Dynamics in Proteins by NMR Cross-Correlated Dipolar Relaxation and Molecular Dynamics Simulations
Probing Methyl Group Dynamics in Proteins by NMR Cross-Correlated Dipolar Relaxation and Molecular Dynamics Simulations
Nuclear magnetic resonance (NMR) spin relaxation is the most informative approach to experimentally probe the internal dynamics of proteins on the picosecond to nanosecond time scale. At the same time, molecular dynamics (MD) simulations of biological macromolecules are steadily improving through better physical models, enhanced sampling methods, and increased computational power, and they provide exquisite information about flexibility and its role in protein stability...
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[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...
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08-09-2016 02:42 PM
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...
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10-28-2015 05:05 PM
[NMR paper] Nonlinear excitations match correlated motions unveiled by NMR in proteins: a new perspective on allosteric cross-talk.
Nonlinear excitations match correlated motions unveiled by NMR in proteins: a new perspective on allosteric cross-talk.
Nonlinear excitations match correlated motions unveiled by NMR in proteins: a new perspective on allosteric cross-talk.
Phys Biol. 2014 Apr 15;11(3):036003
Authors: Piazza F
Abstract
In this paper we propose a novel theoretical framework for interpreting long-range dynamical correlations unveiled in proteins through NMR measurements. The theoretical rationale relies on the hypothesis that correlated...
Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain
Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain
Abstract Temperature-dependence of protein dynamics can provide information on details of the free energy landscape by probing the characteristics of the potential responsible for the fluctuations. We have investigated the temperature-dependence of picosecond to nanosecond backbone dynamics at carbonyl carbon sites in chicken villin headpiece subdomain protein using a combination of three NMR relaxation rates: 13Cā?² longitudinal rate, and two cross-correlated rates involving dipolar and...
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03-20-2011 07:14 PM
[NMR paper] Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in
Cross-correlated relaxation enhanced 1H13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes.
Related Articles Cross-correlated relaxation enhanced 1H13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes.
J Am Chem Soc. 2003 Aug 27;125(34):10420-8
Authors: Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE
A comparison of HSQC and HMQC pulse schemes for recording (1)H(13)C correlation maps of protonated methyl groups in highly deuterated proteins is presented....
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11-24-2010 09:16 PM
[NMR paper] Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain fold
Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
Related Articles Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
J Am Chem Soc. 2003 May 21;125(20):6032-3
Authors: Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP
There is considerable interest in small proteins that fold very rapidly. These proteins have become attractive targets for both theoretical and computational studies. The...
Slow methyl axes motions in perdeuterated villin headpiece subdomain probed by cross-correlated NMR relaxation measurements
Linear Mode
