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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]
Intramolecular transesterification, resulting in a branched polypeptide. In inteins, the new ester bond is broken by an intramolecular attack by the soon-to-be C-terminal asparagine. Intermolecular transesterification can transfer a whole segment from one polypeptide to another, as is seen in the Hedgehog protein autoprocessing.
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.
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.
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. 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.
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.
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]