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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. Tetrameric protein - Wikipedia

    en.wikipedia.org/wiki/Tetrameric_protein

    Hydrogen bonding networks between subunits has been shown to be important for the stability of the tetrameric quaternary protein structure.For example, a study of SDH which used diverse methods such as protein sequence alignments, structural comparisons, energy calculations, gel filtration experiments and enzyme kinetics experiments, could reveal an important hydrogen bonding network which ...

  4. Protein quaternary structure - Wikipedia

    en.wikipedia.org/.../Protein_quaternary_structure

    Protein quaternary structure Protein quaternary structure[a] is the fourth (and highest) classification level of protein structure. Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits). Protein quaternary structure describes the number and

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    The generation of a protein sequence is much easier than the determination of a protein structure. However, the structure of a protein gives much more insight in the function of the protein than its sequence. Therefore, a number of methods for the computational prediction of protein structure from its sequence have been developed. [39]

  6. Protein dimer - Wikipedia

    en.wikipedia.org/wiki/Protein_dimer

    A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins while a protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is ...

  7. 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]

  8. 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 ...

  9. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    Discovering the tertiary structure of a protein, or the quaternary structure of its complexes, can provide important clues about how the protein performs its function and how it can be affected, i.e. in drug design. As proteins are too small to be seen under a light microscope, other methods have to be employed to determine their structure.