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  2. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)

  3. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    If the helix or sheet hydrogen bonding pattern is too short they are designated as T or B, respectively. Other protein secondary structure assignment categories exist (sharp turns, Omega loops, etc.), but they are less frequently used. Secondary structure is defined by hydrogen bonding, so the

  4. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The alpha helix spiral formation An anti-parallel beta pleated sheet displaying hydrogen bonding within the backbone. Formation of a secondary structure is the first step in the folding process that a protein takes to assume its native structure.

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Two main types of secondary structure, the α-helix and the β-strand or β-sheets, were suggested in 1951 by Linus Pauling. [5] These secondary structures are defined by patterns of hydrogen bonds between the main-chain peptide groups.

  6. 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.

  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 contact map - Wikipedia

    en.wikipedia.org/wiki/Protein_contact_map

    Bifurcated hydrogen bonds and multiple hydrogen bonds between amino acid residues; and intra- and interchain hydrogen bonds are also indicated on the plots. Three classes of hydrogen bondings are distinguished by color-coding; short (distance smaller than 2.5 Å between donor and acceptor), intermediate (between 2.5 Å and 3.2 Å) and long ...

  9. Alpha sheet - Wikipedia

    en.wikipedia.org/wiki/Alpha_sheet

    [1] [2] [3] The hydrogen bonding pattern in an alpha sheet is similar to that of a beta sheet, but the orientation of the carbonyl and amino groups in the peptide bond units is distinctive; in a single strand, all the carbonyl groups are oriented in the same direction on one side of the pleat, and all the amino groups are oriented in the same ...