Abstract
Noncovalent interactions govern how molecules communicate. Mass spectrometry is an important and versatile tool for the analysis of noncovalent complexes (NCX). Electrospray mass spectrometry (ESI-MS) is the most widely used MS technique for the study of NCXs because of its softer ionization and easy compatibility with the solution phase of NCX mixtures. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has also been used to study NCXs. However, successful analysis depends upon several experimental factors, such as matrix selection, solution pH, and instrumental parameters. In this study, we employ MALDI imaging mass spectrometry to investigate the location and formation of NCXs, involving both peptides and proteins, in a MALDI sample spot. [Figure not available: see fulltext.]
Original language | English (US) |
---|---|
Pages (from-to) | 1950-1956 |
Number of pages | 7 |
Journal | Journal of the American Society for Mass Spectrometry |
Volume | 24 |
Issue number | 12 |
DOIs | |
State | Published - Dec 2013 |
Externally published | Yes |
Keywords
- Electrostatic and hydrophobic interactions
- Imaging
- MALDI
- Matrix properties
- Noncovalent complexes
ASJC Scopus subject areas
- Structural Biology
- Spectroscopy