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 relaxation rates of two buried and possibly immobile 19F labelled tryptophan sidechains for the multidomain protein RfaH, in its closed conformation, are in reasonable agreement with the calculated values, only when anisotropic rotational diffusion of the protein is considered. While the sparsity of 19F relaxation data from a limited number of probes precludes the experimental determination of the rotational diffusion tensor here, these results demonstrate the influence of rotational diffusion anisotropy of proteins on 19F NMR relaxation of rigid tryptophan sidechains, while adding to the expanding literature of 19F NMR relaxation data sets in biomolecules.
[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.
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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.
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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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[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.
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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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13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
Abstract Aromatic side chains are prevalent in protein binding sites, perform functional roles in enzymatic catalysis, and form an integral part of the hydrophobic core of proteins. Thus, it is of great interest to probe the conformational dynamics of aromatic side chains and its response to biologically relevant events. Indeed, measurements of 13C relaxation rates in aromatic moieties have a long history in biomolecular NMR, primarily in the context 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.
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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
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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...
19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH
Linear Mode
