Protein-protein and protein-ligand interactions studied by electrospray-ionization mass spectrometry

被引：0
|
作者：
Invernizzi, G. [1 ]
Natalello, A. [1 ]
Smalikova, M. [1 ]
Grandori, R. [1 ]
机构：
[1] Univ Milan, Dept Biosci & Biotechnol, I-20126 Milan, Italy
来源：
PROTEIN AND PEPTIDE LETTERS | 2007年 / 14卷 / 09期
关键词：
electrospray-ionization mass spectrometry; non-covalent complexes; binding analysis; arginine repressor; beta-lactoglobulin; tryptophan-repressor binding protein A;
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Preservation of non-covalent interactions in biopolymer mass spectrometry offers new approaches to binding analysis. Recent work from our laboratory is reviewed here and discussed with reference to recent literature in the field. Three issues are considered in particular: hydrophobically stabilized complexes, pH-dependent transitions, and linked protein-ligand and protein-protein binding equilibria.
引用
收藏
页码：894 / 902
页数：9
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