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Download BL 616 Test 1 study guide. The test will probably have 20 multiple
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BL 616 Test 1 study guide. The test will probably have 20 multiple choice, and about 10 problems with short answers; maybe a passage to read and several Q to answer. Read the PowerPoint slides, paying attention to the Learning Outcomes, and major points emphasized. Review the questions at the ends of the chapters, and the problems discussed during the chapters, including the major patients. See also any extra handouts given (as signal transduction) Ch 4-5 buffers, macromolecules pH, ions in blood, cells; acids vs. bases Bicarbonate buffer and other buffers; Nonvolatile acid in urine: Structures of major macromolecules – be able to draw generic nucleotide, fatty acid, phospholipid, triacylglycerol, glucose, and disaccharide, cAMP, Ch 6-7 amino acids, protein structure Be able to draw generic amino acid, peptide bond between two amino acids You will be provided with a diagram of the amino acid side chains if that is needed Describe the different levels of protein structure – what is quaternary What is difference between a polypeptide and a protein What about transmembrane proteins What kinds of modifications occur to proteins after synthesis? – see also enzyme regulation, signal transduction Some specific proteins to know: myoglobin, hemoglobin, adenylyl cyclase b-adrenergic receptor, sickle cell hemoglobin, Ch 8 enzyme catalysis General features of enzymes: S -> P, enzyme not changed, catalysts Active (catalytic) site and what contributes Enzymes lower activation energy of reaction Six categories of enzymes; Some enzymes are RNA molecules (ribozymes) Ex. Glucokinase reaction; chymotrypsin Coenzyme examples of NAD+, Activation-transfer coenzymes Types of inhibitors: covalent, transition-state analogs Ch 9 Regulation of enzyme activity General mechanisms: Reversible binding inactive site Changing conformation of active site (allosteric, covalent, protein-protein, zymogen) M-M equation plot – what is Km, Vmax Phosphorylation as regulatory (Phosphatases, kinases) Allostery Ex. Protein kinase A, Ca-calmodulin, small G proteins (Ras) Ch 10 Cell structure/ function Describe general features of eukaryotic cell Plasma membrane structure, including structures of phospholipids; where are carbohydrates Plasma membrane function including transport proteins, gated channels, active transport Describe structure/function of organelles and cytoskeleton Ch 11 Signal transduction Describe major chemical messengers and where bind – properties of messenger determine receptor plasma membrane receptors and intracellular signal transduction Kinases and phosphatases Examples: nicotinic Ach receptor is ion channel; acetylcholinesterase Receptor tyrosine kinases, such as EGFR and EGF peptide hormone nuclear hormone receptors (steroid receptors) and estrogen, retinoic acid G-protein coupled (heptahelical) receptors for epinephrine, adrenaline How each kind works: draw the diagrams of a plasma membrane: RTK phosphorylates, binds adaptors and membrane-bound Ras –> Raf… kinase cascades G-protein receptor signals through heterotrimeric G protein – GTP – Adenylyl cyclase – cAMP, PKA which phosphorylates proteins; ex. Glycogen breakdown The PIP pathway -> DAG + IP3, Ca++; phospholipases form both pathways use (ch 18 cancer essentials): Oncogenes (proto-oncogenes) vs. tumor suppressors and examples of each: Connection between signal transduction pathways and mutants predisposing to cancer Ras, EGFR, p53, Brca1, cyclin-CDK, Rb, E2F, Cancer is stepwise changes – cell proliferates G1->S critical stage in cell cycle