Download BL 616 Test 1 study guide. The test will probably have 20 multiple

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