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  2. Microscopic reversibility - Wikipedia

    en.wikipedia.org/wiki/Microscopic_reversibility

    The Newton and the Schrödinger equations in the absence of the macroscopic magnetic fields and in the inertial frame of reference are T-invariant: if X(t) is a solution then X(-t) is also a solution (here X is the vector of all dynamic variables, including all the coordinates of particles for the Newton equations and the wave function in the configuration space for the Schrödinger equation).

  3. Detailed balance - Wikipedia

    en.wikipedia.org/wiki/Detailed_balance

    A Markov process is called a reversible Markov process or reversible Markov chain if there exists a positive stationary distribution π that satisfies the detailed balance equations [13] =, where P ij is the Markov transition probability from state i to state j, i.e. P ij = P(X t = j | X t − 1 = i), and π i and π j are the equilibrium probabilities of being in states i and j, respectively ...

  4. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    There is a continuum of inhibitor behaviors spanning reversibility and irreversibility at a given non-arbitrary assay time frame. There are inhibitors that show slow-onset behavior and most of these inhibitors, invariably, also show tight-binding to the protein target of interest.

  5. Dissociation constant - Wikipedia

    en.wikipedia.org/wiki/Dissociation_constant

    The dissociation constant is commonly used to describe the affinity between a ligand (such as a drug) and a protein; i.e., how tightly a ligand binds to a particular protein. Ligand–protein affinities are influenced by non-covalent intermolecular interactions between the two molecules such as hydrogen bonding , electrostatic interactions ...

  6. Protein dynamics - Wikipedia

    en.wikipedia.org/wiki/Protein_dynamics

    The presence of multiple domains in proteins gives rise to a great deal of flexibility and mobility, leading to protein domain dynamics. [1] Domain motions can be inferred by comparing different structures of a protein (as in Database of Molecular Motions ), or they can be directly observed using spectra [ 13 ] [ 2 ] measured by neutron spin ...

  7. Immunostaining - Wikipedia

    en.wikipedia.org/wiki/Immunostaining

    Micrograph of a GFAP immunostained section of a brain tumour.. In biochemistry, immunostaining is any use of an antibody-based method to detect a specific protein in a sample. . The term "immunostaining" was originally used to refer to the immunohistochemical staining of tissue sections, as first described by Albert Coons in 1941.

  8. Hammond's postulate - Wikipedia

    en.wikipedia.org/wiki/Hammond's_postulate

    George Hammond developed the postulate during his professorship at Iowa State University. Hammond's postulate (or alternatively the Hammond–Leffler postulate), is a hypothesis in physical organic chemistry which describes the geometric structure of the transition state in an organic chemical reaction. [1]

  9. Transmembrane protein - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_protein

    Schematic representation of transmembrane proteins: 1) a single-pass membrane protein 2) a multipass membrane protein (α-helix) 3) a multipass membrane protein β-sheet. The membrane is represented in light yellow. A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane.