Bio102: Introduction to Cell Biology and Genetics Fluid Mosaic Model Key Terms: Fluid Mosaic Model Protein Amino Acid Peptide Bond Amino Terminus Carboxyl Terminus Hydrolysis Reaction Condensation Reaction Denaturation Primary Structure Secondary Structure Tertiary Structure Quaternary Structure Hydrogen bonding van der Waals interactions Ionic interactions Disulfide bridges Transmembrane domain Key Questions: How is a membrane “fluid”? What types of movement happen and which types don’t happen? How are individual amino acids different from each other? How are they the same? How are they connected? How is a protein’s three-dimensional structure determined? Why is that structure important? How can that structure be altered? How are proteins integrated into a lipid bilayer? Lecture Outline: Fluid Mosaic Model Proteins within the lipid bilayer Proteins are polymers of amino acids Structure of amino acids side chains are highly variable Peptide bonds to connect amino acids directionality of the polymer – amino terminus is front, carboxyl terminus is back Primary structure is the sequence of the amino acids Secondary structure is 3D shape over short distances Tertiary structure is 3D shape over the entire protein Quaternary structure is the interaction of multiple proteins with each other Secondary-Quaternary structures are determined by noncovalent interactions hydrogen bonding van der Waals interactions ionic interactions disulfide bridges (covalent) Denaturation of proteins destroys their secondary – quaternary structure Sequence determines structure. Structure determines function. Membrane Proteins hydrophobic parts of the protein fit into the hydrophobic environment hydrophillic parts of the protein stick out into the cytosol or outside of cell Proteins and lipids are free to move laterally within the membrane