Amino Acids and Proteins
Carbs and Lipids
pH and ΔG
Metabolic Pathways
Enzymes
100

This amino acid is the only one without a chiral center

What is glycine
100

Glucose and galactose differ only at carbon 4. This makes them this type of stereoisomer

What are epimers

100

When a weak acid and its conjugate base are present in equal amounts this relationship can be used to easily solve a problem

What is pKa=pH when [A-]=[HA]

100

This metabolic pathway converts pyruvate into lactate in the absence of oxygen, regenerating NAD⁺ for glycolysis.

What is lactic acid fermentation

100

This type of enzyme inhibition occurs when a molecule binds to the active site, competing with the substrate.

What is competitive inhibition

200

What is the name of the bond that is created when two cysteine residues undergo oxidation and reinforce a proteins tertiary structure

What are disulfide bonds

200

The bond formed between two monosaccharides is called this specific type of covelant linkage

What is a glycosidic bond

200

A buffer works best near this specific value related to its conjugate acid, often seen on a titration curve plateau

What is the pKa

200

Breaking down one molecule of glucose through glycolysis produces this net amount of ATP, NADH, and pyruvate.

What is 2 ATP,2 NADH, and 2 Pyruvate

200

When substrate binding changes an enzyme’s shape to enhance catalysis, this model explains the interaction.

What is the induced fit model

300

These four amino acids are aromatic...

What is Tryptophan, Phenylalanine, Tryosine, and Histidine

300

This fatty acid feature raises melting temperature while this one lowers it

What are longer chain lengths (increase Tm) and more double bonds (lowers Tm)

300

This term represents the change in free energy of a reaction and predicts whether a reaction will occur spontaneously.

What is Gibbs free energy

300

If 7 Acetyl-CoA molecules were to enter the Citric acid cycle, approximately how much ATP could be generated?

What is 70

21x2.5=52.5

7x1.5=10.5

7x1=7

300

This term represents the substrate concentration at which an enzyme works at half its maximum velocity (Vmax).

What is Km

400

This amino acid has a pKa near physiological pH (~6.0), allowing it act as both a proton donor and acceptor and is most commonly found in the active site of enzymes

What is Histidine

400

This class of lipids consists of four fused hydrocarbon rings and includes cholesterol and many hormones

What are steroids

400

In a reaction preparing acetate buffer, the pKa of acetic acid is 4.76 and the buffer contains .3M acetic acid and .10M sodium acetate. What is the pH?

pH=pKa+log([HA]/[A−])

pH=4.46

400

Gluconeogenesis uses precursors like pyruvate, lactate, or glycerol. To synthesize one glucose from two pyruvate molecules, this is the net ATP/GTP and NADH/NADPH cost.

What is... 4 ATP, 2 GTP, 2 NADH

4 ATP: 2 ATP from pyruvate → oxaloacetate  + 2 ATP from 3-phosphoglycerate → 1,3-bisphosphoglycerate

2 GTP: 2 GTP from oxaloacetate → PEP 

2 NADH: 2 NADH from 1,3-bisphosphoglycerate → glyceraldehyde-3-phosphate 

400

In this process The end product of a pathway inhibits an early enzyme to maintain balance. 

What is Feedback/Allosteric inhibition

500

This term describes independently folded functional units within a single protein that often have distinct roles

What are domains

500

This type of lipid found exclusively on the extracellular side of the plasma membrane and are essential for cell to cell signalling

What are glycolipids

500

A reaction has a ΔG°′ of +5.0 kJ/mol. At 298 K, the [products]=.02M while the [Reactants]=.1M. This term describes how this reaction will proceed.

ΔG = ΔG°′ + RT ln Q

What is non-spontaneous

500

These three enzymes are essential in glycolysis but are irreversible

What are Hexokinase, Phosphofructose kinase, and pyruvate kinase.

500

This inhibition lowers Vmax but leaves Km unchanged

What is noncompetitive inhibition

Why?: Noncompetitive inhibitors bind away from the active site, changing enzyme shape. This reduces the total number of active enzymes, lowering Vmax, but the substrate’s affinity for the active site (Km) doesn’t change.