enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Rotamer - Wikipedia

    en.wikipedia.org/wiki/Rotamer

    Protein side chains exhibit rotamers, whose distribution is determined by their steric interaction with different conformations of the backbone. This effect is evident from statistical analysis of the conformations of protein side chains in the Backbone-dependent rotamer library .

  3. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    A protein fold refers to the general protein architecture, like a helix bundle, β-barrel, Rossmann fold or different "folds" provided in the Structural Classification of Proteins database. [11] A related concept is protein topology.

  4. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...

  5. Conformational change - Wikipedia

    en.wikipedia.org/wiki/Conformational_change

    A change in protein conformation produces a change in the net orientation of the dye relative to the surface plane and therefore the intensity of the second harmonic beam. In a protein sample with a well-defined orientation, the tilt angle of the probe can be quantitatively determined, in real space and real time.

  6. Protein dynamics - Wikipedia

    en.wikipedia.org/wiki/Protein_dynamics

    A network of alternative conformations in catalase (Protein Data Bank code: 1gwe) with diverse properties. Multiple phenomena define the network: van der Waals interactions (blue dots and line segments) between sidechains, a hydrogen bond (dotted green line) through a partial-occupancy water (brown), coupling through the locally mobile backbone (black), and perhaps electrostatic forces between ...

  7. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    The Dictionary of Protein Secondary Structure, in short DSSP, is commonly used to describe the protein secondary structure with single letter codes. The secondary structure is assigned based on hydrogen bonding patterns as those initially proposed by Pauling et al. in 1951 (before any protein structure had ever been experimentally determined).

  8. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and John Kendrew in 1958, for which they received a Nobel Prize in Chemistry A biomolecule or biological molecule is loosely defined as a molecule produced by a living organism and essential to one or more typically biological processes . [ 1 ]

  9. 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 ...