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Updated: Oct 12, 2025

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

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Conformational stability, dynamics and function of human frataxin: Tryptophan side chain interplay

Lucía D Espeche1, Karl Ellioth Sewell2, Ignacio H Castro2

  • 1Departamento de Diagnóstico Genético, Centro Nacional de Genética Médica "Dr. Eduardo E. Castilla" A.N.L.I.S., Av. Las Heras 2670, C1425ASQ, C.A.B.A, Argentina.

Archives of Biochemistry and Biophysics
|November 21, 2021
PubMed
Summary

Investigating frataxin variants revealed that specific tryptophan mutations impact iron-sulfur cluster assembly. Altered protein dynamics, particularly at Trp155, affect the supercomplex

Keywords:
Conformational stabilityFrataxinIron-sulfur cluster assemblyProtein-protein interaction

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