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  2. List of biophysically important macromolecular crystal structures

    en.wikipedia.org/wiki/List_of_biophysically...

    The myoglobin 3-dimensional structure is made up of 8 alpha-helices, and the crystal structure showed that their conformation was right-handed and very closely matched the geometry proposed by Linus Pauling, with 3.6 residues per turn and backbone hydrogen bonds from the peptide NH of one residue to the peptide CO of residue i+4.

  3. Lattice protein - Wikipedia

    en.wikipedia.org/wiki/Lattice_protein

    Download as PDF; Printable version; In other projects ... (2-dimensional to 3-dimensional, for example) of the lattice. [2] ... modeling the protein conformation ...

  4. Biomolecular structure - Wikipedia

    en.wikipedia.org/wiki/Biomolecular_structure

    Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.

  5. 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.

  6. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein dynamics and conformational changes allow proteins to function as nanoscale biological machines within cells, often in the form of multi-protein complexes. [14] Examples include motor proteins, such as myosin, which is responsible for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules ...

  7. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    A protein folded into its native state or native conformation typically has a lower Gibbs free energy (a combination of enthalpy and entropy) than the unfolded conformation.A protein will tend towards low-energy conformations, which will determine the protein's fold in the cellular environment.

  8. Structural genomics - Wikipedia

    en.wikipedia.org/wiki/Structural_genomics

    An example of a protein structure from Protein Data Bank.. Structural genomics seeks to describe the 3-dimensional structure of every protein encoded by a given genome.This genome-based approach allows for a high-throughput method of structure determination by a combination of experimental and modeling approaches.

  9. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    Moreover, the typical secondary structure prediction methods do not account for the influence of tertiary structure on formation of secondary structure; for example, a sequence predicted as a likely helix may still be able to adopt a beta-strand conformation if it is located within a beta-sheet region of the protein and its side chains pack ...