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The sequence of the amino acids in the polypeptide backbone is known as the primary structure of the protein. Like almost all polymers, protein fold and twist, forming into the secondary structure, which is rigidified by hydrogen bonding between the carbonyl oxygens and amide hydrogens in the backbone, i.e. C=O---HN. Further interactions ...
The hydroxyl of tyrosine can deprotonate at high pH forming the negatively charged phenolate. Because of this one could place tyrosine into the polar, uncharged amino acid category, but its very low solubility in water matches the characteristics of hydrophobic amino acids well.
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.
Step-growth polymers increase in molecular weight at a very slow rate at lower conversions and reach moderately high molecular weights only at very high conversion (i.e., >95%). Solid state polymerization to afford polyamides (e.g., nylons) is an example of step-growth polymerization.
In the diagram below, consider the amino-acids as single aliphatic monomers reacting with identical molecules to form a polyamide, focusing on solely the amine and acid groups. Ignore the substituent R groups – under the assumption the difference between the R groups are negligible: The reaction of two amino acids.
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
Glycine N-carboxyanhydride is the parent member of the amino acid N-carboxyanhydrides. NCAs are typically prepared by phosgenation of amino acids: [4] They were first synthesized by Hermann Leuchs by heating an N-ethoxycarbonyl or N-methoxycarbonyl amino acid chloride in a vacuum at 50-70 °C: [5] [6]
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 ...