Waiting
Login processing...

Trial ends in Request Full Access Tell Your Colleague About Jove
Journal / Biochemistry / Kemisk ændring af Tryptofanrester i en…
JoVE Journal
Biochemistry
Author Produced

A subscription to JoVE is required to view this content.

JoVE Journal Biochemistry
Kemisk ændring af Tryptofanrester i en Rekombinant Ca2+-ATPase N-domæne til undersøgelse af Tryptofan-ANS FRET
Hydrolysis of a Ni-Schiff-Base Complex Using Conditions Suitable for Retention of Acid-labile Protecting Groups
Journal (Biochemistry)
Hydrolysis of a Ni-Schiff-Base Complex Using Conditions Suitable for Retention of Acid-labile Protecting Groups
Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy
Journal (Biochemistry)
Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy
 
Click here for the English version

Kemisk ændring af Tryptofanrester i en Rekombinant Ca2+-ATPase N-domæne til undersøgelse af Tryptofan-ANS FRET

Article DOI: 10.3791/62770-v • 12:07 min • October 9th, 2021
October 9th, 2021 •
1, 1
1Instituto de Física, Universidad Autónoma de San Luis Potosí

Chapters

Summary
Automatic Translation

Please note that all translations are automatically generated.

Click here for the English version.

ANS binder sig til Ca2+-ATPase rekombinant N-domæne. Fluorescensspektre viser et FRET-lignende mønster ved excitation ved en bølgelængde på 295 nm. NBS-medieret kemisk modifikation af Trp slukker fluorescensen af N-domæne, hvilket fører til fraværet af energioverførsel (FRET) mellem Trp-restkoncentrationerne og ANS.

Tags

Biokemi udgave 176
Read Article

Get cutting-edge science videos from JoVE sent straight to your inbox every month.

Waiting X
Simple Hit Counter