Biochemistry 2280A Lecture Notes - Lecture 4: Intrinsically Disordered Proteins, Alpha Helix, Protein Folding
28 Oct 2016
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Concerns the 3-d arrangement of a single polypeptide chain. Definition: distinct region of a protein rest of the protein. Many proteins made up of connected domains. Related domains often found in different proteins. Domain folds itself and possess a particular function. Kinase: an enzyme that adds a phosphate onto a substrate: phosphorylates. Take 2 alpha helices and wind them around each other. ~ 3. 6aa per turn contact with water) Hydrophobic residues shielded from water: side chains help to zip them up into a coiled-coil. Helices that are wrapped around each other. Things added to protein after its been made and coiled up: reversible. Phosphorylation, ubiquitination, acetylation, sumoylation alters stability or signaling. Glycosylation affects protein folding, secretion, solubility, binding to other biomolecules: addition of sugar groups to the protein. Myristoylation, farnesylation alters location of a protein: addition of a lipid (hydrophobic molecule) to the protein, lipid doesn(cid:495)t want to interact with water so it finds a membrane and inserts into the.
