Transient state kinetics tutorial using the kinetics simulation program, KINSIM.
This article provides an introduction to a computer tutorial on transient state kinetics. The tutorial uses our Macintosh version of the computer program, KINSIM, that calculates the time course of reactions. KINSIM is also available for other popular computers. This program allows even those investigators not mathematically inclined to evaluate the rate constants for the transitions between the intermediates in any reaction mechanism. These rate constants are one of the insights that are essential for understanding how biochemical processes work at the molecular level. The approach is applicable not only to enzyme reactions but also to any other type of process of interest to biophysicists, cell biologists, and molecular biologists in which concentrations change with time. In principle, the same methods could be used to characterize time-dependent, large-scale processes in ecology and evolution. Completion of the tutorial takes students 6-10 h. This investment is rewarded by a deep understanding of the principles of chemical kinetics and familiarity with the tools of kinetics simulation as an approach to solve everyday problems in the laboratory.
Wachsstock
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Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Pollard
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D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D055592:Biophysical Phenomena; D001703:Biophysics; D003198:Computer Simulation; D003194:Computer-Assisted Instruction; D003285:Contractile Proteins; D004798:Enzymes / Q000378:metabolism; D007700:Kinetics; D008840:Microfilament Proteins / Q000378:metabolism; D008956:Models, Chemical; D051304:Profilins; D011485:Protein Binding; D011487:Protein Conformation; D012984:Software
D000199:Actins; D003285:Contractile Proteins; D004798:Enzymes; D008840:Microfilament Proteins; D051304:Profilins; D000255:Adenosine Triphosphate