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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
Epoxide monomers may be cross linked with themselves, or with the addition of a co-reactant, to form epoxy; BPA is the monomer precursor for polycarbonate; Terephthalic acid is a comonomer that, with ethylene glycol, forms polyethylene terephthalate. Dimethylsilicon dichloride is a monomer that, upon hydrolysis, gives polydimethylsiloxane.
Proteins can bind to other proteins as well as to small-molecule substrates. When proteins bind specifically to other copies of the same molecule, they can oligomerize to form fibrils; this process occurs often in structural proteins that consist of globular monomers that self-associate to form rigid fibers.
All polymers are made of repetitive units called monomers. Biopolymers often have a well-defined structure, though this is not a defining characteristic (example: lignocellulose ): The exact chemical composition and the sequence in which these units are arranged is called the primary structure , in the case of proteins.
An ideal chain (or freely-jointed chain) is the simplest model in polymer chemistry to describe polymers, such as nucleic acids and proteins.It assumes that the monomers in a polymer are located at the steps of a hypothetical random walker that does not remember its previous steps.
Many macromolecules are polymers of smaller molecules called monomers. The most common macromolecules in biochemistry are biopolymers ( nucleic acids , proteins , and carbohydrates ) and large non-polymeric molecules such as lipids , nanogels and macrocycles . [ 1 ]
Polymers range from familiar synthetic plastics such as polystyrene to natural biopolymers such as DNA and proteins that are fundamental to biological structure and function. Polymers, both natural and synthetic, are created via polymerization of many small molecules, known as monomers.
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]