Related Experiment Video
Updated: Aug 9, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
Published on: January 5, 2024
Relationship between the time-dependence of a transient-state kinetic isotope effect and the location of complexes in
Harvey F Fisher1, Bruce A Palfey, Steven J Maniscalco
1Laboratory of Molecular Biochemistry, Veterans Affairs Medical Center, Department of Biochemistry, University of Kansas Medical Center, 4801 Linwood Blvd., Kansas City, Missouri 64128-2226, USA. hfisher@kumc.edu
Abstract:
We prove here a new transient-state kinetic rule which states that the ratios of the first derivatives of kinetic isotope effect time courses, extrapolated to zero time, provide integral values which specify the precise step number in the reaction sequence in single isotope substituted reactions. This rule defines such absolute numbers even where the steps involved are too fast to provide measurable concentrations of intermediates and when the full reaction sequence is unknown.
Related Concept Videos
Transition State Theory
Consecutive Reactions
Predicting Reaction Outcomes
Temperature Dependence on Reaction Rate
Atoms, molecules, or ions must collide before they can react with each other. Atoms must be close together to form chemical bonds. This premise is the basis for a theory that explains many observations regarding chemical kinetics, including factors affecting reaction rates.
The collision theory is based on the postulates that (i) the reaction rate is proportional to the rate of reactant collisions, (ii) the reacting species collide in an orientation allowing contact between...
The Integrated Rate Law: The Dependence of Concentration on Time
Reversible or Opposing Reactions

