Protocol for determining protein dynamics using FT-IR spectroscopy

被引：2
|
作者：
Shen, Hao [1 ,2 ]
Fu, Cuiping [3 ]
Zhang, Junting [3 ]
Feng, Bin [1 ,2 ]
Yu, Shaoning [1 ,2 ]
机构：
[1] Ningbo Univ, Inst Mass Spectrometry, Sch Mat Sci & Chem Engn, Ningbo 315211, Zhejiang, Peoples R China
[2] Ningbo Univ, State Key Lab Managing Biot & Chem Threats Qual &, Ningbo 315211, Peoples R China
[3] Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China
来源：
STAR PROTOCOLS | 2023年 / 4卷 / 04期
基金：
中国国家自然科学基金;
关键词：
HYDROGEN-DEUTERIUM EXCHANGE; CAP-DNA COMPLEX; MASS-SPECTROMETRY; CRYSTAL-STRUCTURE; RECEPTOR PROTEIN; CAMP; KINASE; ACTIVATION; TRANSITION; RESOLUTION;
D O I：
10.1016/j.xpro.2023.102587
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
In biological systems, protein function depends on spatial and temporal changes known as protein dynamics, which can be probed by amide hydrogen/deuterium (H/D) exchange. Here, we present a protocol for determining protein dynamics by Fourier-transform infrared (FT-IR) spectroscopy. We describe steps for pro-tein sample preparation and FT-IR spectra collection. We then detail procedures for spectra analysis. Applications include the effects of protein mutation or pro-tein and metal ion or ligand interactions on the protein H/D exchange rate. For complete details on the use and execution of this protocol, please refer to Yu et al. (2013).1
引用
收藏
页数：23
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