Biochem Block 1: Amino Acids (Fulop)

Front 1

general amino acid structure

Back 1

alpha carbon with r group, hydrogen, carboxyl group, amino group

Front 2

What is a zwitterion?

Back 2

at physiological pH, the amino group is protonated and the carboxyl group is deprotonated

Front 3

how does pH/pKa determine if an amino acid is protonated or deprotonated?

Back 3

pH < pKa = group is protonated
pH > pKa = group is deprotonated
pH = pKa - half is deprotonated, half is protonated

Front 4

Are amino acids that build proteins in the human body in the L or D configuration?

Back 4

L

Front 5

How many proteinogenic amino acids are there in humans?

Back 5

21

Front 6

The amino acid _________ needs the genetic code and a secondary structure in mRNA to be incorporated into proteins

Back 6

selenocysteine

Front 7

name 2 nonproteinogenic amino acids

Back 7

citrulline and ornithine

Front 8

What are the basic amino acids? What are the acidic amino acids?

Back 8

Basic - lys, arg, his. basic lies are his.

acidic - glu asp.

Front 9

Hydrophobic amino acids?

Back 9

Aromatic - phe tyr trp (thea-tyr is a trip)

nonpolar - gly ala pro val leu ile met

Front 10

which amino acid has sulfur?

Back 10

methionine (met)

Front 11

Which hydrophobic amino acid has a rigid secondary structure helpful in introducing kinks in the protein chain?

Back 11

proline

Front 12

What are the polar amino acids?

Back 12

Thr Ser Glu Asp Sec Cys

(three sirs glued asps sel-encysted)

Front 13

What are the polar amino acids with sulfur?

Back 13

selenocysteine, cysteine

Front 14

Which polar amino acids can be glycosylated (oligosacchirides can be attached), further increasing solubility of the amino acid?

Back 14

serine, threonine and asparagine

Front 15

What amino acid is found in proteins with antioxidant activity?

Back 15

selenocysteine

Front 16

which amino acid is helpful in forming disulfide bonds?

Back 16

cysteine

Front 17

what is cystine?

Back 17

a dimer of two cysteines, connected by a disulfide bond

Front 18

In the disease _______, the kidney is unable to reabsorb cystine and basic amino acids from the urine due to a deficient transporter. This causes the formation of cystine stones in the kidney which can be dissolved in alkaline pH

Back 18

cystinuria

Front 19

basic and acidic amino acids act to bind ___________. what's a famous example

Back 19

metal ions. histidine binds Fe2+ in hemoglobin

Front 20

Amino acids can interact with one another in what three ways?

Back 20

1. hydrophobic interactions (van der Waals) - Phenylalanine w/Phenylalanine because both are hydrophobic
2. Ionic interactions between charged amino acids - Glu with Lys
3. hydrogen bonds

Front 21

What determines the primary structure of a protein?

Back 21

the genetic code

Front 22

Variant regions in the primary structure of a protein react in what way to changes? What about invariant

Back 22

they tolerate certain amount of changes without significant changes in protein functions

invariant regions usually form binding sites on proteins, and any changes in these regions drastically alter function