Author : Mowei Zhou
Publisher :
Page : 242 pages
File Size : 38,20 MB
Release : 2013
Category :
ISBN :
Abstract: There is a growing interest in application of mass spectrometry as a high throughput technique for quaternary structure studies of protein complexes. One way to study protein complexes by mass spectrometry is to specifically label peptides segments that carry critical structural information, and after protein digestion subsequently identify the labeled peptides using liquid chromatography - mass spectrometry. A chemical crosslinker forms covalent bonds at specific amino acid sidechains that are in proximity in the protein structure. This approach is used to probe the binding interface of LexA/RecA proteins in Escherichia coli (Chapter 3). In contrast, intact noncovalent protein complexes can be directly transferred into the gas phase, while retaining memory of their solution structures. Accurate molecular weight measurement by mass spectrometry can be used for stoichiometry determination of protein-protein and protein-ligand systems, as manifested by the two examples of stoichiometry determination of differently treated adiponectin oligomers (Chapter 4), and the silver binding properties of the N-terminal region of a bacterial protein CusB (Chapter 5).