Leveraging ultraviolet photodissociation and spectroscopy to investigate peptide and protein three-dimensional structure with mass spectrometry.
Recent advances in mass spectrometry and lasers have facilitated the development of novel experiments combining the benefits of both technologies. This minireview focuses on the coupling of visible/ultraviolet photons with mass spectrometry for analysis of peptide and protein three-dimensional structure. Practical aspects of instrument design and the relationship between experiment and theory are discussed. Experiments utilizing spectroscopy, action spectroscopy, excitation energy transfer, photodissociation, and photoactivated radical chemistry are described. The strengths and weaknesses of each approach are discussed in relation to the type of information typically obtained. A significant body of data suggests that under appropriate source conditions, kinetically trapped structures are observed in these experiments rather than true gas phase minima, suggesting retention of solution phase structural features is possible. Further refinement and exploration of these methods promises to accelerate protein structure discovery in the near future.
Department of Chemistry, University of California, Riverside, 501 Big Springs Road, Riverside, CA 92521, USA. ryan.julian@ucr.edu.
Nathan G
NG
Hendricks
Ryan R
RR
Julian
D007477:Ions; D013058:Mass Spectrometry; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013057:Spectrum Analysis; D014466:Ultraviolet Rays
D007477:Ions; D010455:Peptides; D011506:Proteins