Tryptophan-ANS FRET Study by Modifying ATPase N-domain of Trp Residue | Protocol Preview

Watch the Full Video at https://www.jove.com/v/62770/chemical-modification-tryptophan-residue-recombinant-ca2-atpase-n?utm_source=youtube&utm_medium=social_global&utm_campaign=reseach-videos-2022.

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET – a 2 minute Preview of the Experimental Protocol

José G. Sampedro, Yolanda Cataño
Universidad Autónoma de San Luis Potosí, Instituto de Física;

ANS binds to the Ca2+-ATPase recombinant N-domain. Fluorescence spectra display a FRET-like pattern upon excitation at a wavelength of 295 nm. NBS-mediated chemical modification of Trp quenches the fluorescence of the N-domain, which leads to the absence of energy transfer (FRET) between the Trp residue and ANS.

Visit https://www.jove.com?utm_source=youtube&utm_medium=social_global&utm_campaign=reseach-videos-2022 to explore our entire library of 14,000+ videos of laboratory methods and science concepts.

JoVE is the world-leading producer and provider of science videos with the mission to improve scientific research and education. Millions of scientists, educators, and students at 1500+ institutions worldwide, including schools like Harvard, MIT and Stanford benefit from using JoVE’s extensive library of 14,000+ videos in their research,education and teaching.

Subscribe to our channel: https://www.youtube.com/c/JoVEJournalofVisualizedExperiments