Amino Acids
Enzymes
Structure
Functions
Miscellaneous
100

Name the structurally most simple amino acid.

Glycine

100

The “lock and key” theory of enzymes describes _____.

Enzyme specificity

100

Name the type of bond that helps form alpha helices.

Hydrogen bond

100

High heat and low pH can cause this occur, which renders a protein non-functional.

Denaturation

100

The term used to describe an amino acid at a pH where the protonated and unprotonated forms are equal, giving the molecule a net charge of 0.

Zwitterion

200

Name the 5 components of an amino acid.

Central carbon

Hydrogen atom

Amino group

Carboxyl group

R-group (side chain)


200

This enzyme is able to break bonds without using water.

Lyase

200

Name the type of bond that holds amino acids together.

Peptide bond

200

Enzymes make reactions occur faster by _____.

Lowering activation energy

200

Vitamins are essential to organisms because they function as _____.

Coenzymes

300

A chain of amino acids favors this configuration due to steric hindrance.

Trans

300

In this type of inhibition the inhibitor can bind equally well to the enzyme whether or not the substrate is bound.

Noncompetitive

300

The level of structure formed when multiple polypeptide chains come together to form a protein.

Quaternary

300

Name the class of proteins that regulate the activity of cells and organs and usually travel by blood. (Not all of them are proteins, but many are)

Hormones

300

Ricin exhibitis its toxicity by inhibiting _____.

Ribosomes

400

The body preferentially absorbs amino acids in this conformation.

L

400

Name the enzyme that charges tRNAs.

Aminoacyl-tRNA synthetase
400

Name the covalent bond formed when 2 sulfur atoms from 2 amino acids come together.

Disulfide bond

400

Name the protein found in muscle tissue that contains a heme group that binds oxygen.

Myoglobin

400

What does the Edman degradation procedure of proteins accomplish?

Removes one AA at a time from the N-terminus

500

Name the aromatic amino acids.

Tyrosine

Phenylalanine

Tryptophan

500

The kcat/km of an enzyme tells us _____.

Catalytic efficiency

(How apply an enzyme binds and how quickly it turns over)

500

Beta sheets are formed when amino acids come together in this configuration.

Alternating hydrophilic and hydrophobic AAs

500

Name the class of proteins that are insoluble in water, resistant to digestion, and provide support to tissues.

Fibrous proteins

500

Name the 3 most commonly phosphorylated amino acids.

Serine

Threonine

Tyrosine

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