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Updated: Feb 21, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Calcium-induced changes in annexin V behaviour in solution as seen by proton NMR spectroscopy
J M Neumann1, A Sanson, A Lewit-Bentley
1Département de Biologie Cellulaire et Moléculaire, URA CNRS 1290, CEA Saclay, Gif sur Yvette, France.
Abstract:
The behaviour of human annexin V in the presence of calcium was studied by NMR. We observe the formation of well defined dimers, as well as a change in the local dynamics of one His side chain. We assign the observed changes to either His98 or His267 residues and conclude that they could be related either to the hinge-bending motion reported from crystal structures, or to a local side chain rearrangement within the calcium-binding loops concerned. Dimerization was also confirmed by a small-angle neutron-scattering experiment. Under the experimental conditions used, we do not observe the conformational change involving Trp187 seen in previous studies, which occurs at higher relative calcium concentrations.
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