University Study Skills

Draw the general amino acid structure in its zwitterionic form.

Classify amino acid side chains by charge, polarity, aromaticity, and chemical reactivity.

Predict the protonation state of an ionizable amino acid group from its pKa and the solution pH.

Calculate the net charge of an amino acid or short peptide at a specified pH.

Calculate the isoelectric point of an amino acid with an ionizable side chain.

Draw peptide-bond formation and label the N-terminus, C-terminus, and residue side chains.

Draw a short peptide from its one-letter or three-letter sequence.

Predict how an amino acid substitution changes the local chemical properties of a peptide.

Outline a protein-purification workflow from cell disruption through final analysis.

Select buffer conditions that preserve a target protein's charge state and stability during purification.

Predict protein binding and elution behavior in ion-exchange chromatography.

Predict protein elution order in size-exclusion chromatography.

Explain how affinity chromatography selectively captures and releases a target protein.

Interpret an SDS-PAGE gel to assess protein size and sample purity.

Calculate total activity, specific activity, percent yield, and purification fold from a purification table.

Design a sequence of purification steps using a target protein's size, charge, and binding properties.

Distinguish primary, secondary, tertiary, and quaternary levels of protein structure in molecular representations.

Identify the hydrogen-bonding patterns of alpha helices and beta sheets.

Use a Ramachandran plot to judge whether backbone conformations are sterically allowed.

Predict whether an amino acid side chain is likely to occur in a protein core, on its surface, or in a membrane-spanning region.

Explain how noncovalent interactions and disulfide bonds stabilize a folded protein.

Interpret a protein denaturation curve to estimate stability and unfolding transitions.

Predict how a specified mutation could alter protein folding, stability, or binding.

Interpret common protein structure representations to identify domains, subunits, ligands, and binding sites.

Explain how enzymes accelerate reactions without changing the reaction equilibrium.

Explain how transition-state stabilization contributes to enzyme catalysis.

Calculate initial reaction velocity using the Michaelis–Menten equation.

Interpret Km, Vmax, and kcat as quantitative properties of an enzyme-catalyzed reaction.

Estimate Km and Vmax from initial-rate data or a Michaelis–Menten plot.

Distinguish competitive, uncompetitive, and noncompetitive inhibition from changes in apparent Km and Vmax.

Calculate catalytic efficiency and compare enzymes using kcat/Km.

Predict how pH, temperature, substrate concentration, or an active-site mutation affects enzyme activity.

Draw a nucleotide and distinguish its base, sugar, phosphate, and phosphodiester linkage.

Distinguish DNA from RNA using sugar chemistry, bases, strand structure, and chemical stability.

Write the complementary antiparallel strand for a specified DNA or RNA sequence.

Predict how base composition and solution conditions affect nucleic-acid duplex stability.

Identify the template strand, coding strand, promoter, and transcription direction in a gene diagram.

Trace RNA synthesis through transcription initiation, elongation, and termination.

Compare the core features of bacterial and eukaryotic transcription.

Predict how a promoter mutation or RNA-processing defect changes the resulting transcript.

Translate an mRNA sequence into its corresponding amino acid sequence.

Determine the anticodon and amino acid carried by a tRNA for a specified codon.

Explain how aminoacyl-tRNA synthetases establish translation accuracy.

Trace tRNA movement and peptide-bond formation through one ribosomal elongation cycle.

Explain how start and stop codons control translation initiation and termination.

Predict the protein-level effect of silent, missense, nonsense, and frameshift mutations.

Draw a fatty acid and classify it by chain length, saturation, and cis-trans geometry.

Distinguish triacylglycerols, glycerophospholipids, sphingolipids, and sterols from their structures.

Predict how fatty-acid composition and cholesterol affect membrane fluidity and permeability.

Explain why amphipathic lipids spontaneously form bilayers in water.

Distinguish integral, peripheral, and lipid-anchored membrane proteins.

Compare simple diffusion, facilitated diffusion, primary active transport, and secondary active transport.

Calculate the free-energy change for moving an uncharged solute across a concentration gradient.

Predict transport direction from coupled ion and solute gradients in a cotransporter.

Classify a monosaccharide by carbon number and aldose or ketose chemistry.

Assign D or L configuration and identify epimers from Fischer projections.

Convert a simple monosaccharide between Fischer and Haworth representations.

Distinguish alpha and beta anomers in cyclic monosaccharide structures.

Identify the residues, linkage positions, and reducing end in an oligosaccharide.

Determine whether a carbohydrate is a reducing sugar from its structure.

Compare the structures and biological roles of glycogen, starch, cellulose, and chitin.

Interpret carbohydrate nomenclature to draw a specified disaccharide.

Calculate standard free-energy change from enthalpy and entropy values.

Calculate cellular free-energy change using standard transformed free energy and a reaction quotient.

Determine reaction direction and equilibrium status from the sign and magnitude of free-energy change.

Explain how ATP hydrolysis can drive an otherwise unfavorable biochemical reaction.

Calculate free-energy change for a redox reaction from reduction potentials.

Identify the electron-donor and electron-acceptor roles of NADH, NADPH, and FADH2.

Distinguish catabolic from anabolic pathways by their energy and electron-carrier requirements.

Predict how feedback inhibition changes flux through a simple metabolic pathway.

Trace carbon atoms and ATP use from glucose through the energy-investment phase of glycolysis.

Trace carbon atoms, ATP production, and NADH production through the energy-payoff phase of glycolysis.

Calculate the net ATP, NADH, and pyruvate yield of glycolysis for a specified amount of glucose.

Draw the structures of the major phosphorylated intermediates that explain energy coupling in glycolysis.

Identify the irreversible steps of glycolysis and explain their regulatory significance.

Predict how changes in ATP, AMP, or fructose-2,6-bisphosphate affect glycolytic flux.

Compare lactate and alcoholic fermentation as mechanisms for regenerating NAD+.

Predict metabolite changes caused by inhibiting a specified glycolytic enzyme.

Trace electron flow from NADH or FADH2 to oxygen through the mitochondrial electron-transport chain.

Identify which electron-transport complexes pump protons and relate pumping to electron-transfer energy.

Predict electron-transfer direction using standard reduction potentials.

Explain how the proton-motive force links electron transport to ATP synthesis.

Describe how ATP synthase converts proton flow into chemical-bond energy.

Estimate ATP production from specified amounts of NADH and FADH2 using given P/O ratios.

Predict the effects of respiratory inhibitors and uncouplers on oxygen consumption, the proton gradient, and ATP production.

Explain how electron leakage produces reactive oxygen species and how cells limit oxidative damage.