MASS-SPECTROMETRY AS A READOUT OF PROTEIN-STRUCTURE AND FUNCTION

Citation
Rl. Winston et Mc. Fitzgerald, MASS-SPECTROMETRY AS A READOUT OF PROTEIN-STRUCTURE AND FUNCTION, Mass spectrometry reviews, 16(4), 1997, pp. 165-179
Citations number
83
Language
INGLESE
art.tipo
Review
Journal title
ISSN journal
0277-7037
Volume
16
Issue
4
Year of publication
1997
Pages
165 - 179
Database
ISI
SICI code
0277-7037(1997)16:4<165:MAAROP>2.0.ZU;2-R
Abstract
Proteins have evolved to carry out very specific functions within the cell by interacting with a diverse set of biomolecules. Understanding how a protein's higher order structure relates to its function is impo rtant for defining the molecular basis of these interactions. In recen t years, mass spectrometry has become an important tool for dissecting protein structure and function. Using electrospray ionization (ESI)- and matrix-assisted laser desorption/ionization (MALDI)-based approach es, it has been possible to monitor protein folding, characterize nonc ovalent protein complexes, and assess the contribution of individual a mino acid residues to a protein's function. Here, it is our goal to su mmarize these approaches and highlight recent, biologically relevant a pplications where mass spectrometry has provided unique insight into t he mysteries of protein structure and function. (C) 1998 John Wiley & Sons, Inc., Mass Spectrom Rev 16, 165-179, 1997.