Probing protein dynamics using temperature jump relaxation spectroscopy.
There have been recent advances in initiating and perturbing chemical reactions on very fast timescales, as short as picoseconds, thus making it feasible to study a vast range of chemical kinetics problems that heretofore could not be studied. One such approach is the rapid heating of water solutions using laser excitation. Laser-induced temperature jump relaxation spectroscopy can be used to determine the dynamics of protein motion, an area largely unstudied for want of suitable experimental and theoretical probes, despite the obvious importance of dynamics to protein function. Coupled with suitable spectroscopic probes of structure, relaxation spectroscopy can follow the motion of protein atoms over an enormous time range, from picoseconds to minutes (or longer), and with substantial structural specificity.
Callender
Robert
R
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA. call@aecom.yu.edu
Dyer
R Brian
RB
D004798:Enzymes / Q000737:chemistry; D007700:Kinetics; D008024:Ligands; D009243:NAD / Q000737:chemistry; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013053:Spectrophotometry; D013816:Thermodynamics
D004798:Enzymes; D008024:Ligands; D011506:Proteins; D009243:NAD