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The three individual polypeptide chains that make up the trimer are shown. In biochemistry, a protein trimer is a macromolecular complex formed by three, usually non-covalently bound, macromolecules like proteins or nucleic acids. A protein trimer often occurs from the assembly of a protein's quaternary structure. [1]
Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration (the native state) would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most ...
Depolymerization is a very common process. Digestion of food involves depolymerization of macromolecules, such as proteins.It is relevant to polymer recycling.Sometimes the depolymerization is well behaved, and clean monomers can be reclaimed and reused for making new plastic.
Chemical structure of a polypeptide macromolecule. A macromolecule is a very large molecule important to biological processes, such as a protein or nucleic acid. It is composed of thousands of covalently bonded atoms. Many macromolecules are polymers of smaller molecules called monomers.
When multiple copies of a polypeptide encoded by a gene form a complex, this protein structure is 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 ...
An assemblage of multiple copies of a particular polypeptide chain can be described as a homomer, multimer or oligomer. Bertolini et al. in 2021 [8] presented evidence that homomer formation may be driven by interaction between nascent polypeptide chains as they are translated from mRNA by nearby adjacent ribosomes.
In the simplest model of 'nucleated polymerization' (marked by red arrows in the figure below), individual unfolded or partially unfolded polypeptide chains (monomers) convert into a nucleus (monomer or oligomer) via a thermodynamically unfavourable process that occurs early in the lag phase. [56]
The smallest unit forming a homo-oligomer, i.e. one protein chain or subunit, is designated as a monomer, subunit or protomer. The latter term was originally devised to specify the smallest unit of hetero-oligomeric proteins, but is also applied to homo-oligomeric proteins in current literature.