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  2. Beta-sandwich - Wikipedia

    en.wikipedia.org/wiki/Beta-sandwich

    Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). [ 1 ] The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds.

  3. Protein fold class - Wikipedia

    en.wikipedia.org/wiki/Protein_fold_class

    All-β proteins are a class of structural domains in which the secondary structure is composed entirely of β-sheets, with the possible exception of a few isolated α-helices on the periphery. Common examples include the SH3 domain , the beta-propeller domain , the immunoglobulin fold and B3 DNA binding domain .

  4. Immunoglobulin domain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_domain

    The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids. The backbone switches repeatedly between the two β

  5. Beta sheet - Wikipedia

    en.wikipedia.org/wiki/Beta_sheet

    Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation .

  6. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    Many experimental folding studies have contributed much to our understanding, but the principles that govern protein folding are still based on those discovered in the very first studies of folding. Anfinsen showed that the native state of a protein is thermodynamically stable, the conformation being at a global minimum of its free energy.

  7. Rossmann fold - Wikipedia

    en.wikipedia.org/wiki/Rossmann_fold

    The Rossmann fold is a tertiary fold found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD +, and NADP +.This fold is composed of alternating beta strands and alpha helical segments where the beta strands are hydrogen bonded to each other forming an extended beta sheet and the alpha helices surround both faces of the sheet to produce a three-layered sandwich.

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  9. Template:Alpha beta structure - Wikipedia

    en.wikipedia.org/wiki/Template:Alpha_beta_structure

    This template is intended for use on protein secondary structure pages. To insert, use {{Alpha beta structure}}. On the Alpha helix and Beta sheet pages, it displays alternative versions of the image with the relevant section highlighted. Alternatively, for the non-interactive image, use [[File:Alpha beta structure (full).png]]