BIOL130 Lecture Notes - Lecture 2: Amine, Stereoisomerism, Electronegativity
4 Feb 2020
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Functions: enzymes catalysts, transport through cell membranes, support cytoskeleton, signalling hormones, movement flagella, defense antibodies. Amino acid structure an amino group and a carboxyl group joined with an a-carbon atom alongside a r-group: when ionized, at ph. 7, amino group gains proton and carboxyl group loses an electron amino acid has a central atom which is chiral because it has 4 substituents, this allows for stereoisomers (l & d) Amino acid side chains: nonpolar - hydrophobic, no charged or electronegative atoms to for h bonds insoluble, polar - hydrophilic, soluble, uncharged partial charges can make h bonds, charged contains acids or bases highly soluble. Peptide bond: when two amino acids connect using condensation reaction, the c and n atoms connect making a rigid peptide bond that does not rotate. Polypeptide chain the peptide chain is counted from left to right, n-term to c-term if the primary sequence is changed, the shape and function also change.
