May 4th, 2020
•Lanthipeptide synthetases catalyze multistep reactions during the biosynthesis of peptide natural products. Here, we describe a continuous, bottom-up, hydrogen-deuterium exchange mass spectrometry (HDX-MS) workflow that can be employed to study the conformational dynamics of lanthipeptide synthetases, as well as other similar enzymes involved in peptide natural product biosynthesis.
Tags
Related Videos
Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
Lipid Droplet Isolation for Quantitative Mass Spectrometry Analysis
Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
Optimal Preparation of Formalin Fixed Samples for Peptide Based Matrix Assisted Laser Desorption/Ionization Mass Spectrometry Imaging Workflows
Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
Nitropeptide Profiling and Identification Illustrated by Angiotensin II
A Plasma Sample Preparation for Mass Spectrometry using an Automated Workstation
Sample Preparation for Probe Electrospray Ionization Mass Spectrometry
Copyright © 2024 MyJoVE Corporation. 판권 소유