A

B

C

D

Carboxyl group, Amino group, Bound to same (alpha) carbon. And differs in side chains (R-groups).

Hydroxyl group, Phosphate group, Attached to same beta carbon

Methyl group, Sulfhydryl group, Linked to same gamma carbon

Carbonyl group, Amino group, Connected via same peptide bond

Starts from alpha carbon and goes down the R-group.

Begins at the carboxyl group and ends at the amino group.

Starts from the peptide bond and ends at the terminal nitrogen.

Begins at the beta carbon and follows the hydrogen atoms.

They all have hydrophobic side chains with varying size and shapes.

They all contain aromatic rings and are highly reactive.

They are polar and form hydrogen bonds with water with varying size and shapes.

They all have charged side chains that interact with anions.

Planar, relatively non-polar, and side chains absorb uv light at 270-280 nm.

Highly polar, charged, and form ionic bonds with water molecules.

Non-planar, saturated, and do not interact with UV light.

Contain aliphatic chains and are classified as non-polar aliphatic amino acids.

Side chains are hydrophilic and of varying sizes. Often forms hydrogen bonds.

Side chains are hydrophobic and repel water molecules.

All contain aromatic rings and absorb UV light strongly.

They are charged at physiological pH and form ionic bonds.

They are hydrophilic side chains with a significantly positive charge at pH 7.0

They are nonpolar and repel water molecules.

They carry a negative charge at physiological pH, 7.0.

They are neutral and do not participate in ionic interactions at pH 7.0.

They are hydrophilic side chains with a mostly negative charge at pH 7.0.

They are nonpolar and do not interact with water molecules.

They carry a positive charge at 7.0 pH and stabilize DNA

They are neutral and participate only in hydrophobic interactions.

Carboxyl group is protonated; Amino group is protonated; Net charge of +1

Carboxyl group is deprotonated; Amino group is neutral; Net charge of –1

Both groups are deprotonated; Net charge is 0

Carboxyl group is negatively charged; Amino group is positively charged; Net charge is 0

Carboxyl group is deprotonated; Amino group is protonated; Net Charge of 0, zwitterionic

Carboxyl group is protonated; Amino group is deprotonated; Net charge of +1.

Both groups are deprotonated; Net charge of –1.

Carboxyl group is neutral; Amino group is neutral; Net charge of 0.

Carboxyl group is deprotonated; Amino group is protonated; Net Charge of -1, anionic

Carboxyl group is protonated; Amino group is protonated; Net charge of +1

Both groups are neutral; Net charge of 0

Carboxyl group is deprotonated; Amino group is deprotonated; Net charge of +1

At the pKa of the side chain only.

Between the pKa of the amino and carboxyl groups; pI without side chains considered.

Below the pKa of both the amino and carboxyl groups.

Above the pKa of both the amino and carboxyl groups.

A

B

C

D

E

Alpha carboxyl groups and amino groups destabilize the zwitterion due to charge repulsion.

Alpha carboxyl groups are less acidic than carboxylic acids, and amino groups are more basic than amines.

Alpha carboxyl groups are much more acidic than carboxylic acids, and amino groups are slightly less basic than amines. Works to stabilize zwitterion.

Alpha carboxyl and amino groups behave identically to isolated carboxylic acids and amines.

Alters functional group of the side chain; essential for protein function.

It determines the DNA sequence of the protein.

It breaks down proteins into amino acids for digestion.

It transports proteins directly into the nucleus without any signaling.

Ionic bonds formed between nitrogen and oxygen atoms.

Hydrogen bonds that permanently fuse amino acids into a crystal structure.

Metallic bonds that allow proteins to conduct electricity.

Covalent, peptide bonds, producing linear peptide chains.

An amide functional group.

A glucose molecule to initiate carbohydrate synthesis.

A sulfur bridge that connects DNA strands.

A helium atom to stabilize protein folding in outer space.

Use the Fibonacci sequence to approximate residue count based on protein shape.

Count the number of nitrogen atoms and subtract 42.

Divide its molecular weight by 110.

Multiply the protein’s length by Avogadro’s number.

Activity refers to the enzyme’s mood; specific activity is how many compliments it receives per minute.

Activity is the total units of enzyme in solution. Specific Activity is the number of enzyme units per milligram of total protein.

Activity measures how fast a protein dances under UV light; specific activity tracks its rhythm.

Activity is the number of DNA strands produced; specific activity is the number of RNA strands per cell.

1

2

3

Extreme heat and acid exposure to dissolve all proteins instantly.

Use of radioactive isotopes to scare away unwanted proteins.

High-pressure centrifugation until proteins spontaneously organize by zodiac sign.

Mild conditions; # of different proteins should decease and approach 1