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  2. Loop modeling - Wikipedia

    en.wikipedia.org/wiki/Loop_modeling

    Loop modeling is a problem in protein structure prediction requiring the prediction of the conformations of loop regions in proteins with or without the use of a structural template. Computer programs that solve these problems have been used to research a broad range of scientific topics from ADP to breast cancer .

  3. Hydrophobic-polar protein folding model - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic-polar_protein...

    All amino acid types are classified as either hydrophobic (H) or polar (P), and the folding of a protein sequence is defined as a self-avoiding walk in a 2D or 3D lattice. The HP model imitates the hydrophobic effect by assigning a negative (favorable) weight to interactions between adjacent, non-covalently bound H residues.

  4. Homology modeling - Wikipedia

    en.wikipedia.org/wiki/Homology_modeling

    Homology model of the DHRS7B protein created with Swiss-model and rendered with PyMOL. Homology modeling, also known as comparative modeling of protein, refers to constructing an atomic-resolution model of the "target" protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein (the "template").

  5. 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).

  6. I-TASSER - Wikipedia

    en.wikipedia.org/wiki/I-TASSER

    I-TASSER (Iterative Threading ASSEmbly Refinement) is a bioinformatics method for predicting three-dimensional structure model of protein molecules from amino acid sequences. [1] It detects structure templates from the Protein Data Bank by a technique called fold recognition (or threading). The full-length structure models are constructed by ...

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    This structure is determined by the amino-acid sequence or primary structure. [2] The correct three-dimensional structure is essential to function, although some parts of functional proteins may remain unfolded, [3] indicating that protein dynamics are important. Failure to fold into a native structure generally produces inactive proteins, but ...

  8. Structural bioinformatics - Wikipedia

    en.wikipedia.org/wiki/Structural_bioinformatics

    Lines: each amino acid residue is represented by thin lines, which allows a low cost for graphic rendering. Surface: in this visualization, the external shape of the molecule is shown. Sticks: each covalent bond between amino acid atoms is represented as a stick. This type of visualization is most used to visualize interactions between amino ...

  9. List of protein structure prediction software - Wikipedia

    en.wikipedia.org/wiki/List_of_protein_structure...

    Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure. This list of protein structure prediction software summarizes notable used software tools in protein structure prediction, including homology modeling, protein threading, ab initio methods, secondary structure prediction, and transmembrane helix and signal peptide prediction.