BIO-0013 Chapter Notes - Chapter 3: Peptide Bond, Amine, Chief Operating Officer
22 Sep 2016
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Carboxyl group: cooh, coo-, acid: donates a proton. Peptide bond: c of carboxyl group + n of amino group. R-group orientation: r-groups extend out of peptide backbone, can interact. Flexibility: single bonds on either side of peptide bond can rotate. Structural support for examples collagen saddle-shaped doughnut-shaped cells/tissues. Forms a pore, allows hydrophilic molecules to pass through cell membrane. Primary structure: unique sequence of amino acids in protein. Frederick sanger: each protein has unique sequence of amino acids. 20n combinations of amino acid residues, length n. Stabilized by: hydrogen bonding: o on c=o, h on n-h: alpha helix. Residues are 4 linear positions apart: beta pleated sheet. R-group interactions: hydrogen bonding: polar r + peptide backbone/polar r, hydrophobic interactions: water + hydrophilic rhydrophobic r coalesce, van der waal s interactions: electron movementpartial charges in nonpolar, covalent bonding: disulfide bond- forms bridges, strong links.
