相关实验视频

Updated: Aug 8, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

通过平衡交换取样本的本地蛋白质的罕见波动

Michele Vendruscolo1, Emanuele Paci, Christopher M Dobson

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Journal of the American Chemical Society
|December 18, 2003
PubMed
概括

我们开发了一种新的方法来研究蛋白质结构,使用交换实验和蒙特卡洛模拟. 这种方法揭示了低概率的蛋白质结构,这对于理解蛋白质动态和功能至关重要.

更多相关视频

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

A Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) Platform for Investigating Peptide Biosynthetic Enzymes11:32

A Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) Platform for Investigating Peptide Biosynthetic Enzymes

Published on: May 4, 2020

相关概念视频

¹H NMR of Labile Protons: Temporal Resolution01:10

¹H NMR of Labile Protons: Temporal Resolution

Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...