Protein dynamics from time resolved UV Raman spectroscopy.
Raman spectroscopy can provide unique information on the evolution of structure in proteins over a wide range of time scales; the picosecond to millisecond range can be accessed with pump-probe techniques. Specific parts of the molecule are interrogated by tuning the probe laser to a resonant electronic transition, including the UV transitions of aromatic residues and of the peptide bond. Advances in laser technology have enabled the characterization of transient species at an unprecedented level of structural detail. Applications to protein unfolding and allostery are reviewed.
Balakrishnan
Gurusamy
G
Department of Chemistry, University of Washington, Seattle, WA 98195, United States.
Weeks
Colin L
CL
Ibrahim
Mohammed
M
Soldatova
Alexandra V
AV
Spiro
Thomas G
TG
D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012542:Scattering, Radiation; D012680:Sensitivity and Specificity; D013059:Spectrum Analysis, Raman / Q000379:methods*; D013816:Thermodynamics; D014466:Ultraviolet Rays
D011506:Proteins