NUR1 200 Lecture Notes - Lecture 3: Mutation, Extracellular Fluid, Heme
13 Apr 2015
School
Department
Course
Professor
Document Summary
Ionization characteristics: at nh3+ (amino terminal) or bottom coo- (carboxyl terminal: amino acid residue has r group that can be ionized: coo- (at right) Post translational modification of peptides: that change allows for a better affinity with cell receptors. Calcitonin has an intra chain disulfide bond: forming between 2 cys and an amid terminal (ppt slide 7) Represents a molecule with all its parts and contours. Eg (image to the right): substrate is the enzyme with an active site. Configuration where molecule is at lowest energy level and most stable. Molecule in a physiological state will fold into that native configuration. Typical structural patterns observed in protein molecules reflect two basic rules. Hydrophobic aa residues are mostly buried deep inside a protein molecule away from h2o molecules. H bonding within the protein molecule is at a maximum: weak non-covalent interactions: most important to determine the 3-d shape/configuration of a molecule.
