Dissociation rate
The dissociation rate in chemistry, biochemistry, and pharmacology is the rate or speed at which a ligand dissociates from a protein, for instance, a receptor.[1] It is an important factor in the binding affinity and intrinsic activity (efficacy) of a ligand at a receptor.[1] The dissociation rate for a particular substrate can be applied to enzyme kinetics, including the Michaelis-Menten model.[2] Substrate dissociation rate contributes to how large or small the enzyme velocity will be.[2] In the Michaelis-Menten model, the enzyme binds to the substrate yielding an enzyme substrate complex, which can either go backwards by dissociating or go forward by forming a product.[3] The dissociation rate constant is defined using Koff.[2]
References
- ^ a b Wanner, Klaus; Höfner, Georg (27 June 2007). Mass Spectrometry in Medicinal Chemistry: Applications in Drug Discovery. John Wiley & Sons. pp. 142–156. ISBN 978-3-527-61091-4.
{{cite book}}: Unknown parameter|name-list-format=ignored (|name-list-style=suggested) (help) - ^ a b c Berezhkovskii AM, Szabo A, Rotbart T, Urbakh M, Kolomeisky AB (April 2017). "Dependence of the Enzymatic Velocity on the Substrate Dissociation Rate". The Journal of Physical Chemistry B. 121 (15): 3437–3442. doi:10.1021/acs.jpcb.6b09055. PMC 5577799. PMID 28423908.
- ^ Berezhkovskii AM, Szabo A, Rotbart T, Urbakh M, Kolomeisky AB (April 2017). "Dependence of the Enzymatic Velocity on the Substrate Dissociation Rate". The Journal of Physical Chemistry B. 121 (15): 3437–3442. doi:10.1021/acs.jpcb.6b09055. PMC 5577799. PMID 28423908.
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