BCH210H1 Lecture 3: Lecture 3 Notes
15 Sep 2018
School
Course
Professor
49
BCH210H1 Full Course Notes
Verified Note
49 documents
Document Summary
Bch210h1(f) lecture 3: 4 levels of protein structure, primary (1 ): the linear amino acid sequence, ex. the primary structure of insulin: Bch210h1(f) lecture 3: -helix as a whole, -helix from the top: green = side chains of amino acids stick out. H-bonds face interior of helix, while side chains are exposed around the periphery (outside) of the structure. This means that the side chains are going to interact with the environment (water or protein). Actual diameter of alpha helix depends on what the amino acids are: some -helix dimensions, 3. 6 residues/360 turn, 100 between adjacent residues, 1. 5 rise/residue, 5 across backbone. Bch210h1(f) lecture 3: properties of alpha helices depend on side chains: Amphipathic = dual properties: helix-helix interactions are typically anti-parallel, and 50 tilt angle is common, though large helices are typically parallel with respect to one another. Bch210h1(f) lecture 3: -sheet structure formed by anti-parallel strands, putting the strands together gives you the -pleated sheet:
