enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a ...

  3. Disulfide - Wikipedia

    en.wikipedia.org/wiki/Disulfide

    The structure of a disulfide bond can be described by its χ ss dihedral angle between the C β −S γ −S γ −C β atoms, which is usually close to ±90°. The disulfide bond stabilizes the folded form of a protein in several ways: It holds two portions of the protein together, biasing the protein towards the folded topology.

  4. Beta sheet - Wikipedia

    en.wikipedia.org/wiki/Beta_sheet

    Some proteins that are disordered or helical as monomers, such as amyloid β (see amyloid plaque) can form β-sheet-rich oligomeric structures associated with pathological states. The amyloid β protein's oligomeric form is implicated as a cause of Alzheimer's. Its structure has yet to be determined in full, but recent data suggest that it may ...

  5. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    Core residues are often conserved in a protein family, whereas the residues in loops are less conserved, unless they are involved in the protein's function. Protein tertiary structure can be divided into four main classes based on the secondary structural content of the domain. [25] All-α domains have a domain core built exclusively from α ...

  6. Nucleic acid tertiary structure - Wikipedia

    en.wikipedia.org/.../Nucleic_acid_tertiary_structure

    Two important functions are the binding potential with ligands or proteins, and its ability to stabilize the whole tertiary structure of DNA or RNA. The strong structure can inhibit or modulate transcription and replication, such as in the telomeres of chromosomes and the UTR of mRNA. [18] The base identity is important towards ligand binding.

  7. Fixation (histology) - Wikipedia

    en.wikipedia.org/wiki/Fixation_(histology)

    Precipitating (or denaturing) fixatives act by reducing the solubility of protein molecules and often by disrupting the hydrophobic interactions that give many proteins their tertiary structure. The precipitation and aggregation of proteins is a very different process from the crosslinking that occurs with aldehyde fixatives.

  8. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Tertiary structure may give way to the formation of quaternary structure in some proteins, which usually involves the "assembly" or "coassembly" of subunits that have already folded; in other words, multiple polypeptide chains could interact to form a fully functional quaternary protein. [12]

  9. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    A protein structure database is a database that is modeled around the various experimentally determined protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way.