Acid-Base Chemistry
Protein Structure & Function
Membrane Transport
Enzymes
Metabolism
100

This pH range indicates the conditions are acidic.

What is pH < 7?

100

This amino acid's name can be remembered by it's non-polar V-shaped side-chain.

What is valine?

100

This type of transport occurs as a result of a concentration or ionic gradient across a biological membrane.

What is passive transport?

100

An enzyme catalyzes the rate of a reaction by stabilizing (lowering the energy of) this chemical species.

What is the transition state?

100

This describes the chemical change associated with decreasing charge, adding electrons, losing oxygen, and/or adding hydrogens/hydride.

What is reduction?

200

This is the name of the equation that is commonly used to calculate the pH of buffer solutions.

What is the Henderson-Hasselbach equation?

200

This secondary structure forms with hydogen bonding between the backbone C=O of the nth residue and the backbone N-H bond of the (n+4)th residue.

What is an alpha helix?

200

The membrane transporter KscA transports K+ by mimicking this type of environment surrounding the K+.

What is the water hydration shell?

200

This type of enzyme catalyzes bond formation coupled to ATP hydrolysis.

What is a ligase?

200

Steps 1-5 in glycolysis, which consume 2 ATP molecules and generate 2 GAP's, are generally described as this type of "phase."

What is the "investment phase"?

300

This characteristic of a buffer is optimized when the pH = pKa and the concentrations of buffer components are high.

What is the buffer capacity?

300

This driving force for protein folding, which causes entropy to increase, is characterized by the release of water molecules upon forming contacts between non-polar amino acid residues.

What is the hydrophobic effect?

300

To help students remember the distribution of electrolytes in vs. out of the cell, Dr. Allen's phrase, "Cells are like bananas floating in..." ends with this.

What is "salty milk"?

300

During this type of catalysis, and an amino acid in the active site receives a H+ from the substrate.

What is base catalysis?

300

In addition to more resonance structures and solute-solvent interactions, this is responsible for the stabilization of products of ATP hydrolysis.

What is the separation of negative charge (minimization of electrostatic repulsion)?

400

When the pH > pKa, a weak acid is more likely to exist in this form.

What is the de-protonated form?

400

BPG stabilizes this conformational state of hemoglobin by binding to the central cavity.

What is the T-State?

400

The gradient created by the Na+,K+-ATPase is used to drive the Na+,Glucose symporter.  This is an example of this type of transport.

What is secondary active transport?

400

This mathematical quantity, involving kcat and KM, is used to assess the catalytic efficiency of an enzyme.

What is kcat/KM?

400

In the citric acid cycle this substrate oxidizes alcohols to ketones, and then goes on to deliver electrons to the electron-transport chain.

What is NAD+?

500

When the side-chain of histidine is next to a negatively-charged aspartate, the pKa of the histidine side-chain changes in this way.

What is "it increases"?

500

This non-covalent interaction would occur between the side chains of Lys and Ser.

What is an ion-dipole interaction?

500

This amino acid modification occurs in active transporters upon ATP hydrolysis, which is often accompanied by large conformational (structural) changes in the protein.

What is phosphorylation?

500

This type of inhibition only affects the apparent KM (not vmax) in the presence of the inhibitor.

What is competitive inhibition?

500

This type of metabolic regulation involves controlling two separate enzymes for the forward and reverse reaction, in order to regulate the net flux of metabolites.

What is substrate cycling?