Assessing the applicability of ¹⁹F labeled tryptophan residues to quantify protein dynamics

URN to cite this document:: urn:nbn:de:bvb:355-epub-535402
DOI to cite this document:: 10.5283/epub.53540

Krempl, Christina ; Sprangers, Remco

License: Creative Commons Attribution 4.0
PDF - Published Version
(5MB)

Date of publication of this fulltext: 17 Jan 2023 05:30

Alternative links to fulltext:DOI Publisher

This publication is part of the DEAL contract with Springer.

Details

Preview

Indexed in

Export bibliographical data

Abstract

Nuclear magnetic resonance (NMR) spectroscopy is uniquely suited to study the dynamics of biomolecules in solution. Most NMR studies exploit the spins of proton, carbon and nitrogen isotopes, as these atoms are highly abundant in proteins and nucleic acids. As an alternative and complementary approach, fluorine atoms can be introduced into biomolecules at specific sites of interest. These labels ...