BCH210H1 Lecture Notes - Cystine, Imidazole, Indole
49
BCH210H1 Full Course Notes
Verified Note
49 documents
Document Summary
Properties of the protein components: the amino acids. They are zwitterionic as monomers- neutral overall but within the molecule there is a separation in charge (positive and negative) Joined together through peptide bonds- peptide bonds are through dyhydration (removal of h20) c=o attach to nh. Amino acids usually have a chirality center (except gly) the l isomer is usually found in proteins. The side chains of amino acids are either hydrophobic (non-polar) or hydrophilic (polar charge) Hydrophobic amino acids occur usually in the interior of globular proteins. Hydrophilic (polar) amino acids occur on the protein surface (interacts with water) Some residues- especially gly and pro have structural functions in protein chains. Beta- branched- the second carbon is a ch. Hydrophobic amino acids= ala, cys, ile, leu, met, phe, val. Hydrophilic (polar) amino acids= basic: arg, lys acidic: asp, glu polar: asn, gln, his. Mid- range amino acids= ser, thr, tr, trp, gly, pro. Pka= the ph of protonation or de-protonation.
