Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
3.3K Views
•
12:07 min
•
October 9th, 2021
DOI :
October 9th, 2021
•Chapters in this video
0:03
Introduction
1:15
Determination (in silico) of the ANS and SERCA N‐Domain Interaction
3:09
Expression and Purification of the Recombinant N‐Domain
3:39
Monitor the Formation of the ANS‐N‐Domain Complex Based on ANS and N‐Domain Fluorescence Intensity Changes
7:38
N‐Domain Intrinsic Fluorescence Titration by Trp Chemical Modification with NBS
8:43
Titrate the NBS Modified N‐Domain with ANS by Recording Fluorescence Spectra at 25°C
9:37
Evidence of ANS Binding to the Chemically Modified N‐Domain by Excitation at λ = 370 nm
10:32
Results Overview
11:30
Conclusions
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