NUTR 3210 Lecture Notes - Lecture 7: Portal Venous System, Portal Vein, Trypsin Inhibitor

• School: University of Guelph
• Department: Nutrition
• Course: NUTR 3210
• Professor: Genevieve Newton

Document Summary

Amino acid strucure: all have same general structure; only difference between aas are different side chains, amine fu(cid:374)(cid:272)tio(cid:374)al g(cid:396)oup (cid:894)p(cid:396)i(cid:373)a(cid:396)(cid:455) a(cid:373)i(cid:374)e(cid:895), -carbon, h- atom, -cooh function group, side chain. Aas are uncharged; appears to have basic nh2 group and acidic. 4 components: amino terminal (nh2), alpha carbon, carboxyl terminal (cooh), side chain. However at physiological ph, amino groups are protonated. +) and carboxylic acid group is deprotonated (coo-) aa in this (nh3 form is called zwitterions; uncharged b/c positive and negative charge cancel out, thus no overall charge, unless side chain is charged. Molecule is polar at this point and is very water soluble. Unit 7: asparagine neutral amide of aspartate, glutamine neutral amide of glutamate; major inter-organ n carrier important for protein metabolism; source of nh3. Iodination: addition of iodine to synthesize thyroid hormones, regulating metabolic rate: adp-ribosylation: addition of adp-ribose to proteins associated w/ dna repair and protein function; adp-ribosylation elates to niacin (vit b3)