Time-resolved mid-infrared spectroscopy: methods and biological applications.
Recent developments in time-resolved infrared spectroscopy have paved the way to probe transient intermediates with a high degree of functional group specificity on timescales as short as femtoseconds. This capability has been exploited in studies of biophysical phenomena ranging from protein folding/unfolding to ligand migration in proteins.
Slayton
R M
RM
Department of Chemistry & Chemical Biology, Harvard University, Cambridge, MA 02138, USA. slayton@fas.harvard.edu
Anfinrud
P A
PA
D001426:Bacterial Proteins / Q000737:chemistry; D003576:Electron Transport Complex IV / Q000737:chemistry; D010788:Photosynthesis; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013055:Spectrophotometry, Infrared / Q000379:methods*; D013997:Time Factors
D001426:Bacterial Proteins; D011506:Proteins; D003576:Electron Transport Complex IV