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  2. Conformational change - Wikipedia

    en.wikipedia.org/wiki/Conformational_change

    A specific nonlinear optical technique called second-harmonic generation (SHG) has been recently applied to the study of conformational change in proteins. [4] In this method, a second-harmonic-active probe is placed at a site that undergoes motion in the protein by mutagenesis or non-site-specific attachment, and the protein is adsorbed or ...

  3. Structural bioinformatics - Wikipedia

    en.wikipedia.org/wiki/Structural_bioinformatics

    In general, protein structures are classified into four levels: primary (sequences), secondary (local conformation of the polypeptide chain), tertiary (three-dimensional structure of the protein fold), and quaternary (association of multiple polypeptide structures). Structural bioinformatics mainly addresses interactions among structures taking ...

  4. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein domains. The two shown protein structures share a common domain (maroon), the PH domain, which is involved in phosphatidylinositol (3,4,5)-trisphosphate binding. Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds.

  5. Sequential model - Wikipedia

    en.wikipedia.org/wiki/Sequential_model

    The sequential model (also known as the KNF model) is a theory that describes cooperativity of protein subunits. [1] It postulates that a protein's conformation changes with each binding of a ligand, thus sequentially changing its affinity for the ligand at neighboring binding sites.

  6. Conformational ensembles - Wikipedia

    en.wikipedia.org/wiki/Conformational_ensembles

    This movie depicts the 3-D structures of each of the representative conformations of the Markov State Model of Pin1 WW domain. In computational chemistry, conformational ensembles, also known as structural ensembles, are experimentally constrained computational models describing the structure of intrinsically unstructured proteins.

  7. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    A protein folded into its native state or native conformation typically has a lower Gibbs free energy (a combination of enthalpy and entropy) than the unfolded conformation.A protein will tend towards low-energy conformations, which will determine the protein's fold in the cellular environment.

  8. Protein quaternary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_quaternary_structure

    Protein quaternary structure [a] is the fourth (and highest) classification level of protein structure.Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits).

  9. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...