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  2. Protein quaternary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_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.

  3. Zimm–Bragg model - Wikipedia

    en.wikipedia.org/wiki/Zimm–Bragg_model

    In statistical mechanics, the Zimm–Bragg model is a helix-coil transition model that describes helix-coil transitions of macromolecules, usually polymer chains. Most models provide a reasonable approximation of the fractional helicity of a given polypeptide; the Zimm–Bragg model differs by incorporating the ease of propagation (self-replication) with respect to nucleation.

  4. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    1. The recognition of codons by release factors, which causes the hydrolysis of the polypeptide chain from the tRNA located in the P site [1] 2. The release of the polypeptide chain [57] 3. The dissociation and "recycling" of the ribosome for future translation processes [57] A summary table of the key players in translation is found below:

  5. Amyloid - Wikipedia

    en.wikipedia.org/wiki/Amyloid

    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]

  6. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a

  7. Post-translational modification - Wikipedia

    en.wikipedia.org/wiki/Post-translational...

    For instance, the peptide hormone insulin is cut twice after disulfide bonds are formed, and a propeptide is removed from the middle of the chain; the resulting protein consists of two polypeptide chains connected by disulfide bonds. Some types of post-translational modification are consequences of oxidative stress.

  8. Macromolecule - Wikipedia

    en.wikipedia.org/wiki/Macromolecule

    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.

  9. Protein complex - Wikipedia

    en.wikipedia.org/wiki/Protein_complex

    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 ...