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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").
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 .
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.
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).
Amino-acid chains, known as polypeptides, fold to form a protein. Proteins consist of chains of amino acids which spontaneously fold to form the three dimensional (3-D) structures of the proteins. The 3-D structure is crucial to understanding the biological function of the protein.
A target structure (ribbons) and 354 template-based predictions superimposed (gray Calpha backbones); from CASP8. Critical Assessment of Structure Prediction (CASP), sometimes called Critical Assessment of Protein Structure Prediction, is a community-wide, worldwide experiment for protein structure prediction taking place every two years since 1994.
The only required input is a protein sequence for the prediction of the protein 3D structure and function. [1] The IntFOLD output is presented via a user-friendly interface for the use of life scientists. The raw data is also formatted in Critical Assessment of Methods for Protein Structure Prediction (CASP) standards with a detailed help page. [1]
Because protein structures are composed of amino acids whose side chains are linked by a common protein backbone, a number of different possible subsets of the atoms that make up a protein macromolecule can be used in producing a structural alignment and calculating the corresponding RMSD values.