Mass spectrometry as a readout of protein structure and function.
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 important for defining the molecular basis of these interactions. In recent 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 approaches, it has been possible to monitor protein folding, characterize noncovalent protein complexes, and assess the contribution of individual amino acid residues to a protein's function. Here, it is our goal to summarize these approaches and highlight recent, biologically relevant applications where mass spectrometry has provided unique insight into the mysteries of protein structure and function.
Winston
R L
RL
Scripps Research Institute, La Jolla, California 92037, USA.
Fitzgerald
M C
MC
D000595:Amino Acid Sequence; D000818:Animals; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*; D011518:Proto-Oncogene Proteins / Q000737:chemistry; D050737:Proto-Oncogene Proteins c-crk
D011506:Proteins; D011518:Proto-Oncogene Proteins; D050737:Proto-Oncogene Proteins c-crk