19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH

Alam, MK and Bhuvaneshwari, RA and Sengupta, I (2024) 19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH. In: Journal of Biomolecular NMR .

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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 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. © The Author(s), under exclusive licence to Springer Nature B.V. 2024.

Item Type:	Journal Article
Publication:	Journal of Biomolecular NMR
Publisher:	Springer Science and Business Media B.V.
Additional Information:	The copyright for this article belongs to the Publisher.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	19 Nov 2024 20:46
Last Modified:	19 Nov 2024 20:46
URI:	http://eprints.iisc.ac.in/id/eprint/86786

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