Dynamics of liquids, molecules, and proteins measured with ultrafast 2D IR vibrational echo chemical exchange spectroscopy.
A wide variety of molecular systems undergo fast structural changes under thermal equilibrium conditions. Such transformations are involved in a vast array of chemical problems. Experimentally measuring equilibrium dynamics is a challenging problem that is at the forefront of chemical research. This review describes ultrafast 2D IR vibrational echo chemical exchange experiments and applies them to several types of molecular systems. The formation and dissociation of organic solute-solvent complexes are directly observed. The dissociation times of 13 complexes, ranging from 4 ps to 140 ps, are shown to obey a relationship that depends on the complex's formation enthalpy. The rate of rotational gauche-trans isomerization around a carbon-carbon single bond is determined for a substituted ethane at room temperature in a low viscosity solvent. The results are used to obtain an approximate isomerization rate for ethane. Finally, the time dependence of a well-defined single structural transformation of a protein is measured.
Fayer
M D
MD
Department of Chemistry, Stanford University, Stanford, California 94305, USA. fayer@stanford.edu
D002244:Carbon / Q000737:chemistry; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000379:methods*; D013997:Time Factors; D014732:Vibration
D011506:Proteins; D002244:Carbon