Biology And Biomedical Sciences BIOL 2960 Lecture Notes - Lecture 6: Ionic Bonding, Coomassie Brilliant Blue, Keratin
14 Aug 2018
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Document Summary
When you"re done studying for this unit, you should be able to: appreciate the diversity of protein structures that enable proteins to carry out unique functions. In a chemical structure of a peptide, be able to identify and label the peptide bonds, a carbons, amino acid r-groups, hydrogen bond donors/acceptors, and n- and c- termini. Apply your knowledge from last week"s molecular interactions lecture to categorize an amino acid as hydrophobic or hydrophilic and whether it is polar, positively charged (basic), or negatively charged (acidic) when given that amino acid"s r-group structure. Nonpolar = hydrophobic: have mainly hydrocarbon side chains. Polar = hydrophilic: negatively charged=acidic amino acids, positively charged=basic amino acids, polar by uncharged side chains all c"s and h"s with o"s too. Primary: amino acid monomers are joined, forming polypeptide chains and are stabilized by polypeptide bonds. Secondary: polypeptide chains may form alpha-helices or beta pleated sheets and are stabilized by hydrogen bonds.
