The recent application of ^(19)F NMR in the study of biomolecular structure and dynamics has made it a potentially attractive probe to complement traditional ^(15)N/^(13)C labelled probes for backbone and sidechain dynamics, albeit with some complications. The utility of ^(15)N relaxation rates of rigid backbone amide groups to determine the rotational diffusion tensor of proteins is well established. Here we show that the measured ^(19)F relaxation rates of two buried and possibly immobile...
19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH
19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH
Abstract
The recent application of 19F NMR in the study of biomolecular structure and dynamics has made it a potentially attractive probe to complement traditional 15N/13C labelled probes for backbone and sidechain dynamics, albeit with some complications. The utility of 15N relaxation rates of rigid backbone amide groups to determine the rotational diffusion tensor of proteins is well established. Here we show that the measured 19F...
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[NMR paper] Accurate Prediction of Protein NMR Spin Relaxation by Means of Polarizable Force Fields. Application to Strongly Anisotropic Rotational Diffusion.
Accurate Prediction of Protein NMR Spin Relaxation by Means of Polarizable Force Fields. Application to Strongly Anisotropic Rotational Diffusion.
Related Articles Accurate Prediction of Protein NMR Spin Relaxation by Means of Polarizable Force Fields. Application to Strongly Anisotropic Rotational Diffusion.
J Phys Chem B. 2020 Jun 05;:
Authors: Marcellini M, Nguyen MH, Martin M, Hologne M, Walker O
Abstract
Among the various biophysical methods available to investigate protein dynamics, NMR present the ability to scrutinize...
[NMR paper] Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation.
Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation.
Related Articles Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation.
Biophys J. 2018 Jan 23;114(2):392-399
Authors: Awosanya EO, Nevzorov AA
Abstract
A membrane-bound form of Pf1 coat protein reconstituted in magnetically aligned DMPC/DHPC bicelles was used as a molecular probe to quantify for the viscosity of the lipid membrane interior by measuring the uniaxial rotational diffusion...
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Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation
Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation
Publication date: 23 January 2018
Source:Biophysical Journal, Volume 114, Issue 2</br>
Author(s): Emmanuel O. Awosanya, Alexander A. Nevzorov</br>
A membrane-bound form of Pf1 coat protein reconstituted in magnetically aligned DMPC/DHPC bicelles was used as a molecular probe to quantify for the viscosity of the lipid membrane interior by measuring the uniaxial rotational diffusion coefficient of the protein. Orientationally dependent 15N NMR relaxation times in the...
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02-03-2018 02:16 PM
[NMR paper] Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Related Articles Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Chem Commun (Camb). 2017 Aug 25;:
Authors: Gerecht K, Figueiredo AM, Hansen DF
Abstract
Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N?-C? bond of...
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[NMR paper] Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of
Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of HIV-I protease tethered dimer by real time NMR spectroscopy.
Related Articles Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of HIV-I protease tethered dimer by real time NMR spectroscopy.
Biochem Biophys Res Commun. 2000 Mar 16;269(2):387-92
Authors: Panchal SC, Hosur RV
HIV I protease has been the target of extensive and variety of investigations in recent years because of its importance in the AIDS viral life cycle. We...
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[NMR paper] Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxatio
Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields.
Related Articles Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields.
J Biomol NMR. 1996 Oct;8(3):273-84
Authors: Tjandra N, Wingfield P, Stahl S, Bax A
15N NMR relaxation times in perdeuterated HIV-1 protease, complexed with the sub-nanomolar inhibitor DMP323, have been measured at 600 and 360 MHz 1H frequency. The relative magnitudes of the principal...