BSC 300 Lecture Notes - Lecture 4: N-Terminus, Protein Folding, Ionic Bonding

• School: University of Alabama
• Department: Biological Sciences
• Course: BSC 300
• Professor: Yoder

Document Summary

Amino acid side groups and their effect on protein chemistry. Three unique acids: glycine, proline and cysteine. Primary, secondary, tertiary and quarternary structure and the principle bonds/ forces that drive these orders. Secondary structures: (cid:0) - helices vs. (cid:0) - pleated sheets. Proteins: polymers of amino acids forming a diverse group of macromolecules: wide variety of cellular functions with high degree of specificity. Motor: move cargo and drive cell shape change. Storage: reserves of ions and amino acids for cellular activities. Each has a central carbon (the (cid:0) carbon), an amino group, a carboxyl group, and a variable r group. At cellular ph, monomeric amino acids are ionized at both ends. Individual amino acid in a protein = residue. Peptide bonds join amino acids: carboxyl group of one molecule reacts with the amino group of another molecule releasing water (dehydration reaction catalyzed in ribosomes) Not a protein until it is folded into its final native conformation.