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  2. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The favoured model for the enzyme–substrate interaction is the induced fit model. [53] This model proposes that the initial interaction between enzyme and substrate is relatively weak, but that these weak interactions rapidly induce conformational changes in the enzyme that strengthen binding.

  3. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    The model is used in a variety of biochemical situations other than enzyme-substrate interaction, including antigen–antibody binding, DNA–DNA hybridization, and protein–protein interaction. [ 17 ] [ 18 ] It can be used to characterize a generic biochemical reaction, in the same way that the Langmuir equation can be used to model generic ...

  4. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    The Michaelis–Menten Model can be an invaluable tool to understanding enzyme kinetics. According to this model, a plot of the reaction velocity (V 0 ) associated with the concentration [S] of the substrate can then be used to determine values such as V max , initial velocity, and K m (V max /2 or affinity of enzyme to substrate complex).

  5. Metabolic network modelling - Wikipedia

    en.wikipedia.org/wiki/Metabolic_network_modelling

    Enzymes and metabolites are the red dots and interactions between them are the lines. Metabolic network model for Escherichia coli Metabolic network modelling , also known as metabolic network reconstruction or metabolic pathway analysis , allows for an in-depth insight into the molecular mechanisms of a particular organism.

  6. List of unsolved problems in chemistry - Wikipedia

    en.wikipedia.org/wiki/List_of_unsolved_problems...

    Enzyme kinetics: Why do some enzymes exhibit faster-than-diffusion kinetics? [13] Protein folding problem: Is it possible to predict the secondary, tertiary and quaternary structure of a polypeptide sequence based solely on the sequence and environmental information? Inverse protein-folding problem: Is it possible to design a polypeptide ...

  7. Enzyme induction and inhibition - Wikipedia

    en.wikipedia.org/wiki/Enzyme_induction_and...

    Enzyme induction is a process in which a molecule (e.g. a drug) induces (i.e. initiates or enhances) the expression of an enzyme. Enzyme inhibition can refer to the inhibition of the expression of the enzyme by another molecule; interference at the enzyme-level, basically with how the enzyme works.

  8. Supramolecular catalysis - Wikipedia

    en.wikipedia.org/wiki/Supramolecular_catalysis

    The term supramolecular chemistry is defined by Jean-Marie Lehn as "the chemistry of intermolecular bond, covering structures and functions of the entities formed by association of two or more chemical species" in his Nobel lecture in 1987, [5] but the concept of supramolecular catalysis was started way earlier in 1946 by Linus Pauling when he ...

  9. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Whereas the concept of water activity is widely known and utilized in the applied biosciences, its complement—the protein activity which quantitates protein–protein interactions—is much less familiar to bioscientists as it is more difficult to determine in dilute solutions of proteins; protein activity is also much harder to determine for ...