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  2. Protein quaternary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_quaternary_structure

    Protein quaternary structure describes the number and arrangement of multiple folded protein subunits in a multi-subunit complex. It includes organizations from simple dimers to large homooligomers and complexes with defined or variable numbers of subunits. [1] In contrast to the first three levels of protein structure, not all proteins will ...

  3. Disulfide - Wikipedia

    en.wikipedia.org/wiki/Disulfide

    The prototype of a protein disulfide bond is the two-amino-acid peptide cystine, which is composed of two cysteine amino acids joined by a disulfide bond. 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°.

  4. 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]

  5. Beta barrel - Wikipedia

    en.wikipedia.org/wiki/Beta_barrel

    In protein structures, a beta barrel (β barrel) is a beta sheet (β sheet) composed of tandem repeats that twists and coils to form a closed toroidal structure in which the first strand is bonded to the last strand (hydrogen bond). Beta-strands in many beta-barrels are arranged in an antiparallel fashion.

  6. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Quaternary structure is the three-dimensional structure consisting of the aggregation of two or more individual polypeptide chains (subunits) that operate as a single functional unit . The resulting multimer is stabilized by the same non-covalent interactions and disulfide bonds as in tertiary

  7. Biomolecular structure - Wikipedia

    en.wikipedia.org/wiki/Biomolecular_structure

    The primary structure of a biopolymer is the exact specification of its atomic composition and the chemical bonds connecting those atoms (including stereochemistry).For a typical unbranched, un-crosslinked biopolymer (such as a molecule of a typical intracellular protein, or of DNA or RNA), the primary structure is equivalent to specifying the sequence of its monomeric subunits, such as amino ...

  8. Protein dimer - Wikipedia

    en.wikipedia.org/wiki/Protein_dimer

    In biochemistry, a protein dimer is a macromolecular complex or multimer formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word dimer has roots meaning "two parts", di-+ -mer. A protein dimer is a type of protein quaternary structure.

  9. Protein complex - Wikipedia

    en.wikipedia.org/wiki/Protein_complex

    Protein complexes are distinct from multidomain enzymes, in which multiple catalytic domains are found in a single polypeptide chain. [1] Protein complexes are a form of quaternary structure. Proteins in a protein complex are linked by non-covalent proteinprotein interactions. These complexes are a cornerstone of many (if not most ...