BCH210H1 Lecture Notes - Lecture 4: Amide, National Model Railroad Association, Peptide Bond

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Lecture 4: protein structure proteins are classed according to shape and solubility shape: globular or fibrous. Go from n- terminus to c- terminus repeating conformations in the polypeptide chain periodic, repetitive units. Two units together: tetramer. Hemoglobin 2 alpha chains, 2 beta chains = heterotrimer. This protein has 6 different subunits that come together to make a tetramer. When the subunits are the same = homotrimer. When the subunits are different= heterotrimer. Protein structure and function and tightly linked. A protein"s conformation can be described as its overall 3d structure. Nuclear magnetic resonance spectroscopy (nmr) Methods for determining 3d protein structure cilia fibrous proteins: structural/mechanical support. Many are also integral components of membranes/membrane associated proteins. Hemoglobin has 2 different conformations. When its bound to o2, and when its not bound to o2 looks different depending on the binding of oxygen. Correspond to what type of atom they are and what kind of chemical environment they are in.