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  2. Protein dynamics - Wikipedia

    en.wikipedia.org/wiki/Protein_dynamics

    The presence of multiple domains in proteins gives rise to a great deal of flexibility and mobility, leading to protein domain dynamics. [1] Domain motions can be inferred by comparing different structures of a protein (as in Database of Molecular Motions ), or they can be directly observed using spectra [ 13 ] [ 2 ] measured by neutron spin ...

  3. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    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 in some instances, misfolded proteins have modified or toxic functionality.

  4. Conformational change - Wikipedia

    en.wikipedia.org/wiki/Conformational_change

    Kinesin walking on a microtubule is a molecular biological machine using protein domain dynamics on nanoscales Main article: Protein dynamics In biochemistry , a conformational change is a change in the shape of a macromolecule , often induced by environmental factors.

  5. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    Pyruvate kinase, a protein with three domains (In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of ...

  6. 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).

  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. This Is the Exact Amount of Protein You Need to Eat to Lose ...

    www.aol.com/exact-amount-protein-eat-lose...

    In terms of animal-based protein sources, Huggins says that fish, seafood, lean cuts of meat, eggs and Greek yogurt are all good sources because they are high in protein as well as other important ...

  9. Nuclear magnetic resonance spectroscopy of proteins - Wikipedia

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance...

    One important problem using homonuclear nuclear magnetic resonance is overlap between peaks. This occurs when different protons have the same or very similar chemical shifts. This problem becomes greater as the protein becomes larger, so homonuclear nuclear magnetic resonance is usually restricted to small proteins or peptides. [citation needed]