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  2. Conformational ensembles - Wikipedia

    en.wikipedia.org/wiki/Conformational_ensembles

    This movie depicts the 3-D structures of each of the representative conformations of the Markov State Model of Pin1 WW domain. In computational chemistry, conformational ensembles, also known as structural ensembles, are experimentally constrained computational models describing the structure of intrinsically unstructured proteins.

  3. 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).

  4. Levinthal's paradox - Wikipedia

    en.wikipedia.org/wiki/Levinthal's_paradox

    Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration (the native state) would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most ...

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    The generation of a protein sequence is much easier than the determination of a protein structure. However, the structure of a protein gives much more insight in the function of the protein than its sequence. Therefore, a number of methods for the computational prediction of protein structure from its sequence have been developed. [39]

  6. Folding funnel - Wikipedia

    en.wikipedia.org/wiki/Folding_funnel

    The diagram sketches how proteins fold into their native structures by minimizing their free energy. The folding funnel hypothesis is a specific version of the energy landscape theory of protein folding, which assumes that a protein's native state corresponds to its free energy minimum under the solution conditions usually encountered in cells.

  7. Protein design - Wikipedia

    en.wikipedia.org/wiki/Protein_design

    Protein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function. [1] Proteins can be designed from scratch (de novo design) or by making calculated variants of a known protein structure and its sequence (termed protein redesign).

  8. Graphical models for protein structure - Wikipedia

    en.wikipedia.org/wiki/Graphical_models_for...

    To learn the graph structure as a multivariate Gaussian graphical model, we can use either L-1 regularization, or neighborhood selection algorithms. These algorithms simultaneously learn a graph structure and the edge strength of the connected nodes. An edge strength corresponds to the potential function defined on the corresponding two-node ...

  9. Structural bioinformatics - Wikipedia

    en.wikipedia.org/wiki/Structural_bioinformatics

    Calculating contacts is an important task in structural bioinformatics, being important for the correct prediction of protein structure and folding, thermodynamic stability, protein-protein and protein-ligand interactions, docking and molecular dynamics analyses, and so on.