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

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