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  2. CATH database - Wikipedia

    en.wikipedia.org/wiki/CATH_database

    The CATH Protein Structure Classification database is a free, publicly available online resource that provides information on the evolutionary relationships of protein domains. It was created in the mid-1990s by Professor Christine Orengo and colleagues including Janet Thornton and David Jones , [ 2 ] and continues to be developed by the Orengo ...

  3. List of proteins - Wikipedia

    en.wikipedia.org/wiki/List_of_proteins

    Proteins may be classified as to their three-dimensional structure (also known a protein fold). The two most widely used classification schemes are: [2] CATH database [3] Structural Classification of Proteins database (SCOP) [4] Both classification schemes are based on a hierarchy of fold types.

  4. Structural Classification of Proteins database - Wikipedia

    en.wikipedia.org/wiki/Structural_Classification...

    As of February 2015, SCOPe 2.05 classified 71,000 of the 110,000 total PDB entries. [11] SCOP2 prototype was a beta version of Structural classification of proteins and classification system that aimed to more the evolutionary complexity inherent in protein structure evolution. [12]

  5. Lancefield grouping - Wikipedia

    en.wikipedia.org/wiki/Lancefield_grouping

    Bacteria of the genus Enterococcus, formerly known as group D streptococci, were classified as members of the genus Streptococcus until 1984 and are included in the original Lancefield grouping. [4] Many—but not all—species of streptococcus are beta-hemolytic .

  6. Protein fold class - Wikipedia

    en.wikipedia.org/wiki/Protein_fold_class

    Numerous protein structures are the result of rational design and do not exist in nature. Proteins can be designed from scratch (de novo design) or by making calculated variations on a known protein structure and its sequence (known as protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to ...

  7. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).

  8. Protein complex - Wikipedia

    en.wikipedia.org/wiki/Protein_complex

    Kinesin is a protein functioning as a molecular biological machine. It uses protein domain dynamics on nanoscales. A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multidomain enzymes, in which multiple catalytic domains are found in a single polypeptide chain ...

  9. Immunoglobulin superfamily - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_superfamily

    Members of the IgSF include cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins. They are commonly associated with roles in the immune system.

  1. Related searches team name for 4 members of group 2 are classified based on structure of protein

    list of proteins wikipedialist of different proteins