O-Chem
Proteins
Carbohydrates
Enzymes
Random
100

These organic compounds contain a hydroxyl functional group.

alcohols
100

Which amino acid forms intrastrand disulfide bonds?

Cysteine

100

Simple carbohydrates are often named as aldoses or _________.

Ketoses

100

The portion of the enzyme where the reaction takes place is called the: ________ ________.

active site

100

A peptide with a net charge of zero is called the __________.

Zwitterion

200

There are ___ carbons and ___ hydrogens in heptane.

7 carbons, 16 hydrogens

200

This type of structure generally stays intact upon denaturation unless a restriction enzyme is used.

Primary

200

If we are referring to the last chiral carbon, when the -OH is on the right, we call it a ___ carbohydrate.

D

200

Enzymes lower the __________ __________, but do not change delta G of the reaction.

activation energy

200

The pH at which an ionizable group will begin to lose a H atom is called the ____.

pKa

300

This functional group makes the peptide bond in peptides.

amide

300

Myoglobin does not have this level of structure.

Quaternary (it is a monomer)

300

The carbon where alpha or beta carbohydrates are distinguished is called the ________ carbon.

anomeric

300

Describe a competitive inhibitor.

Competes for the actual substrate for the active site.

300

How many essential amino acids are there?

9

400
Name the structure for a 4 carbon chain with a carbonyl at carbon 2.

2-butanone

400

What category of amino acid types do glycine and alanine fall under?

Nonpolar/Hydrophobic

400

We call non-superimposable mirror images __________.

enatiomers

400

This type of enzyme can transfer a group from one thing to another.

Transferase

400

If you infinitely increase the concentration of substrate, will the enzyme work infinitely faster? Answer yes or no and include an explanation.

No - because at some point you will reach the maximum turnover rate for the enzyme and you can only go as fast as diffusion brings substrate into the active site.

500

These two functional groups are present on all amino acids.

amino and carboxyl group

500

Name 3 of the forces that contribute to tertiary structure.

salt bridges, H-bonding, disulfide bonds, hydrophilic or hydrophobic interactions

500

The most common hexose is a building block for lactose and sucrose. It is called ___________ .

D-glucose

500

This type of inhibition may allow substrate to bind to the active site, but will prevent the reaction from proceeding.

noncompetitive inhibition
500

There are three aromatic amino acids that absorb light in the UV-Vis region at 280 nm. Name one of these amino acids.

Tryptophan, Tyrosine, Phenylalanine

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