Acids with Attitude
Inhibition Inquiries
The Encyclopedia of Enzymes
High on Hemoglobin
What about Wild Cards?
100

The amino acid whose side chain only contains a single methyl group

What is Alanine?

100

The type of inhibition that decreases Vmax, but leaves Km unaffected

What is noncompetitive Inhibition?
100

A tightly bound group to an enzyme that is not made of amino acids, but still critical to the function of that enzyme.

What is a prosthetic group?

100

Cooperativity explains this phenomenon in hemoglobin.

What is hemoglobin's ability to bind oxygen easier as more oxygen bind? 


100

The two structures associated with secondary protein structure

What are alpha helices and beta pleated sheets?
200

The amino acid that looks like this:


What is glutamine?

200

The enzyme will experience these changes to Km and Vmax when bound to an uncompetitive inhibitor

What is a decreased Km and Vmax?

200

The enzyme that utilizes a catalytic triad

What is chymotrypsin?

200

This specialized molecule can stabilize the "T" state of hemoglobin

What is 2-3-BPG?

200

A pathogen that solely consists of amino acids

What is a prion?

300

The amino acid responsible for disulfide bonds

What is Cysteine?



300

The site in which a noncompetitive inhibitor will bind to

What is the allosteric site?

300

The maximum speed at which a given enzyme will catalyze a reaction.

What is Vmax?

300

Hemoglobin can bind and release oxygen much easier in this state.

What is the "R" state?

300

The change in entropy as a protein folds.

What is -deltaS?

400

The group of amino acids that generally have a protonated side chain at physiological pH

What are basic amino acids?

400

The condition in which a competitive inhibitor will bind

What is when substrate is not bound to the enzyme?

400

The role of histidine in the chymotrypsin mechanism. (think nucleophile/electrophile, acid/base)

What is a base and acid?

400

The condition that causes sickle-cell hemoglobin to polymerize.

What is the exposing of a hydrophobic patch in sickle cell hemoglobin during the "T" state?

400

The type of secondary structure represented by shading in the top left region of a Ramachandran plot

What are alpha helices?

500

The one-letter code equivalents to this peptide chain:


What is RVY?

500

Uncompetitive inhibition will cause Km to decrease, which by itself will result in this effect on enzyme velocity.

What is increased enzyme velocity?

500

The definition of Km conceptually.

What is the substrate concentration [S] at 1/2 of Vmax?

500

This structure can freely move once an oxygen binds to a hemoglobin monomer, affecting R and T state equilibrium.

What is the alpha helix attached to the heme group?

500
This condition allows for a spontaneous reaction when change in S is negative.

What is when change in enthalpy is negative?