BIOL2000 Lecture Notes - Lecture 2: Lipid Bilayer, Peptide Bond, Hydrogen Bond

• School: Boston College
• Department: Biology
• Course: BIOL2000
• Professor: Stanley Dunn

Document Summary

Peptide bond: carboxyl of one aa bonds to amino of other aa producing h2o. Peptide bond between n and shares electrons like a double bond. Reverse reaction that breaks bonds using water. Protein structure: primary: sequence of amino acid, secondary: h bonding interactions between backbones, tertiary: 3d shape of polypeptide, quaternary: many polypeptide chains make functional protein. Single bonds on sides of peptide bonds can rotate. Helix is stabillized by the h bonds between carboxyl and amide 4 groups away. Beta strands interact to form pleated sheet. Stabilized by h bonds btw carboxyl and amide. Pockets that bind w small molecules inside. Interactions btw 2 or more peptide chains. Polypeptide chain: intramolecular bonds w in same molecule. Vanderwaals : nonpolar, hydrophobic effect: folded into interior: pockets. Ex: single pp may have 1 or 10+ domains. Unfolded aa sequence will still have distinct domains. Kept peptide bond bc covalent but broken noncovalent bonds.