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The Polynucleotides, RNA and DNA, are long polymers of nucleotides. Polypeptides include proteins and shorter polymers of amino acids; some major examples include collagen, actin, and fibrin. Polysaccharides are linear or branched chains of sugar carbohydrates; examples include starch, cellulose, and alginate.
In polymer science, the Lifson–Roig model [1] is a helix-coil transition model applied to the alpha helix-random coil transition of polypeptides; [2] it is a refinement of the Zimm–Bragg model that recognizes that a polypeptide alpha helix is only stabilized by a hydrogen bond only once three consecutive residues have adopted the helical conformation.
Depicted above is the monomeric ELP unit. X represents an arbitrary amino acid. Polymers are formed from this pentapeptide monomeric unite. Elastin-like polypeptides (ELPs) are synthetic biopolymers with potential applications in the fields of cancer therapy, tissue scaffolding, metal recovery, and protein purification.
Both the α-helix and the β-sheet represent a way of saturating all the hydrogen bond donors and acceptors in the peptide backbone. Some parts of the protein are ordered but do not form any regular structures. They should not be confused with random coil, an unfolded polypeptide chain lacking any fixed three-dimensional structure.
In general, polypeptides are unbranched polymers, so their primary structure can often be specified by the sequence of amino acids along their backbone. However, proteins can become cross-linked, most commonly by disulfide bonds , and the primary structure also requires specifying the cross-linking atoms, e.g., specifying the cysteines involved ...
Polymer nomenclature is generally based upon the type of monomer residues comprising the polymer. A polymer which contains only a single type of repeat unit is known as a homopolymer, while a polymer containing two or more types of repeat units is known as a copolymer. [22] A terpolymer is a copolymer which contains three types of repeat units ...
In addition, RNA is a single-stranded polymer that can, like proteins, fold into a very large number of three-dimensional structures. Some of these structures provide binding sites for other molecules and chemically active centers that can catalyze specific chemical reactions on those bound molecules.
Self-assembling peptides are a category of peptides which undergo spontaneous assembling into ordered nanostructures.Originally described in 1993, [1] these designer peptides have attracted interest in the field of nanotechnology for their potential for application in areas such as biomedical nanotechnology, [2] tissue cell culturing, [3] [4] molecular electronics, and more.