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  2. InterPro - Wikipedia

    en.wikipedia.org/wiki/InterPro

    SUPERFAMILY is a library of profile hidden Markov models that represent all proteins of known structure. The library is based on the SCOP classification of proteins: each model corresponds to a SCOP domain and aims to represent the entire SCOP superfamily that the domain belongs to. SUPERFAMILY has been used to carry out structural assignments ...

  3. Category:Proteins by function - Wikipedia

    en.wikipedia.org/wiki/Category:Proteins_by_function

    Pages in category "Proteins by function" The following 9 pages are in this category, out of 9 total. This list may not reflect recent changes. A. Antifreeze protein;

  4. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    Sequence similarity is used to classify proteins both in terms of evolutionary and functional similarity. This may use either whole proteins or protein domains, especially in multi-domain proteins. Protein domains allow protein classification by a combination of sequence, structure and function, and they can be combined in many ways.

  5. 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 ...

  6. Structural Classification of Proteins database - Wikipedia

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

    Proteins having the same shape and some similarity of sequence and/or function are placed in "families", and are assumed to have a closer common ancestor. Similar to CATH and Pfam databases, SCOP provides a classification of individual structural domains of proteins, rather than a classification of the entire proteins which may include a ...

  7. Protein superfamily - Wikipedia

    en.wikipedia.org/wiki/Protein_superfamily

    Some protein dynamics [8] and conformational changes of the protein structure may also be conserved, as is seen in the serpin superfamily. [9] Consequently, protein tertiary structure can be used to detect homology between proteins even when no evidence of relatedness remains in their sequences.

  8. 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).

  9. Protein function prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_function_prediction

    Similar protein sequences, usually indicate shared functions. Proteins of similar sequence are usually homologous [5] and thus have a similar function. Hence proteins in a newly sequenced genome are routinely annotated using the sequences of similar proteins in related genomes. However, closely related proteins do not always share the same ...