Mass spectrometric analysis of cross-linking sites for the structure of proteins and protein complexes.
Mass spectrometry has become the method of choice to detect and quantify the minute amounts of proteins at the genomic scale. It has recently been adopted for three dimensional structure analyses of proteins or protein complexes by chemically cross-linking their intact forms and analyzing the cross-linked pieces after digestion. This highlight provides an overview of the technology with a focus on advances in the last two years. This cross-linking mass spectrometry has a great potential to become a powerful tool to supplement current X-ray and NMR method of protein structure analysis.
Jin Lee
Young
Y
Genome Center, University of California, One Shields Ave, Davis, California 95616, USA. yojlee@ucdavis.edu
D000595:Amino Acid Sequence; D000818:Animals; D003432:Cross-Linking Reagents / Q000737:chemistry*; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods* / Q000639:trends; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D011506:Proteins / Q000737:chemistry*
D003432:Cross-Linking Reagents; D046912:Multiprotein Complexes; D011506:Proteins