Multimers
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Multimers
Protein quaternary structure 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 arrangement of multiple protein folding, folded protein subunits in a Multiprotein complex, multi-subunit complex. It includes organizations from simple protein dimer, dimers to large homooligomers and multiprotein complex, complexes with defined or variable numbers of subunits. In contrast to the first three levels of protein structure, not all proteins will have a quaternary structure since some proteins function as single units. Protein quaternary structure can also refer to biomolecular complexes of proteins with nucleic acids and other Cofactor (biochemistry), cofactors. Description and examples Many proteins are actually assemblies of multiple polypeptide c ...
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Protein Trimer
In biochemistry, a protein trimer is a macromolecular complex formed by three, usually non-covalently bound, macromolecules like proteins or nucleic acids. A homotrimer would be formed by three identical molecules. A heterotrimer would be formed by three different macromolecules. Type II Collagen is an example of homotrimeric protein. Porins usually arrange themselves in membranes as trimers. Bacteriophage T4 tail fiber Multiple copies of a polypeptide encoded by a gene often can form an aggregate referred to as a multimer. When a multimer is formed from polypeptides produced by two different mutant alleles of a particular gene, the mixed multimer may exhibit greater functional activity than the unmixed multimers formed by each of the mutants alone. When a mixed multimer displays increased functionality relative to the unmixed multimers, the phenomenon is referred to as intragenic complementation. The distal portion of each of the bacteriophage T4 tail fibers is encoded by ge ...
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