Biol 2100 Exam 1 Learning Objectives (9/15/2024) - PDF

**Biol 2100 learning objectives rev 9/15/2024** The best way to engage with these learning objectives is to attempt them (explain, predict, describe, draw, calculate, interpret, etc.) with a classmate. Only someone who is familiar with the content may recognize when you've been incomplete or incorr...

**Biol 2100 learning objectives rev 9/15/2024** The best way to engage with these learning objectives is to attempt them (explain, predict, describe, draw, calculate, interpret, etc.) with a classmate. Only someone who is familiar with the content may recognize when you've been incomplete or incorrect. You should be able to do these things without referring to your notes, textbook, or lecture recordings. Identifying *early* what you're not yet capable of doing provides an opportunity to get help and achieve that objective before the exam! [Exam 1] Chemical foundations essential to understanding cellular and molecular biology Explain why the distinction between covalent and non-covalent is important to biologists, and what distinguishes covalent bonds from ionic bonds, hydrogen bonds, van der Waals and hydrophobic interactions Explain the relationship between polar covalent bonds and hydrogen bonds Predict hydrophilicity/hydrophobicity based on chemical structure Recognizing an association as being covalent or non-covalent based on an image or description Recognize on chemical structures where carbon and hydrogen exist but are not shown with C and H symbols (remembering carbon shares 4 electron pairs, see amino acid examples) Protein structure and function Draw the general structure of an amino acid in both ionized and non-ionized forms Model and recognize amino acid isomers (optional, covered in P2L second week) Recognize by structure amino acids with highly hydrophobic or highly hydrophilic side chains Draw or model the effect of pH on amino acids and relation to protein structure and function Identify hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, phosphate, and methyl groups Define monomer, residue, polymer, peptide, polypeptide chain, and protein Define hydrolysis and dehydration/condensation reactions and model with a dipeptide Describe, identify, and note stabilizing forces of primary, secondly, tertiary, & quaternary structure Describe typical location of hydrophobic and hydrophilic sidechains in a protein Illustrate the principles of structural and functional domains ~~ Calculate the number of molecules in a particular volume based on concentration in mass/volume~~ ~~ Interpret SDS-PAGE data~~ (this and the one above will be on exam 2) Cell structure and cytoskeleton Distinguish cytoplasm and cytosol Interpret immunofluorescent microscopy images Describe the structure and functions of microtubules, microfilaments, and intermediate filaments Recognize names of proteins forming microtubules, microfilaments, and associated motor proteins Explain and illustrate the concept of structural polarity and its significance to cytoskeletal filaments List similarities and differences between plant, animal, and prokaryotic cells Lipids and membranes Define lipid and recognize them by their common structural characteristics Define amphipathic noting its relevance to membrane lipids Recognize a phospholipid by its structure and note the common feature of head groups Describe what is meant by membrane asymmetry ~~ Give an example of the significance of the asymmetric distribution of membrane phospholipids~~ Describe variation among membrane lipid tails and relation to permeability Recognize cis- versus trans- double bonds, understanding which are in our membrane lipids and why Describe the role of cholesterol in animal cell membranes Describe the features of molecules that influence their ability to diffuse across cell membrane Membrane transport, endocytosis and exocytosis Recognize integral (transmembrane), peripheral, and lipid-linked membrane proteins Distinguish channels, uniporters, symporters, antiporters, and pumps; describe mechanisms driving active transport (both primary/direct as illustrated by Na+/K+ pump, and secondary/indirect as illustrated by glucose symport) Predict the net flow direction of osmosis using the relative terms hypertonic and hypotonic Explain the effect of electrochemical gradients on the diffusion of solutes Distinguish phagocytosis, pinocytosis, and receptor-mediated endocytosis from one another and from membrane transport of solutes Free energy and coupled reactions Define and relate "free energy", exergonic, endergonic, entropy, enthalpy, endo- and exothermic Describe the influence of enthalpy and entropy changes on ∆G of a reaction or process Predict whether a reaction or process is likely endergonic or exergonic Explain the principle of coupled reactions using a biological example Given ∆G values, determine whether reactions may be effectively coupled Describe what ∆G of a reaction or process does, and does not, tell us Enzymes Explain why thermodynamically favorable reactions won't occur instantaneously Define enzyme, explain why cells use enzymes rather than temperature to regulate reaction rates Explain why enzymes do not change the ∆G of a reaction Describe examples of how enzymes function including the role of co-factors Explain Vmax, Km and how each is influenced by competitive and non-competitive inhibitors Explain why different enzymes have different optimal temperature and pH activity profiles