M1 Biochemistry: 1. Amino Acid Chemistry

Front 1

Amino Acids provide metabolic energy of ____ kcal / g.

Back 1

4 kcal/g

Front 2

The general structure of an amino acid is the charged "zwitterion" form. Describe that structure.

Back 2

Alpha carbon with an amino group, a carboxyl, R group and H.

Front 3

The structure of a general amino acid is called... and looks like...

Back 3

zwitterion

Front 4

Naturally occurring amino acids are almost exclusively [what stereoisomer]?

Back 4

L-stereoisomer

Front 5

Back 5

Gly


Glycine

Hint 5

Nonpolar, alipathic R group

Front 6

Back 6

Ala


Alanine

Hint 6

Nonpolar, alipathic R group

Front 7

Back 7

Pro


Proline

Hint 7

Nonpolar, alipathic R group

Front 8

Back 8

Val


Valine

Hint 8

Nonpolar, alipathic R group

Front 9

Back 9

Leu


Leucine

Hint 9

Nonpolar, alipathic R group

Front 10

Back 10

Ile


Isoleucine

Hint 10

Nonpolar, alipathic R group

Front 11

Back 11

Met


Methionine

Hint 11

Nonpolar, alipathic R group

Front 12

___ amino acids have an α-amino group; _____ is the exception with an α-imino group.

Back 12

19 ; proline is the only one with an α-imino group.

Front 13

Which amino acid is actually an imino acid?

Back 13

Proline - it is the only one that is an imino acid because it has a secondary imine in its structure.

Front 14

Which amino acid has an isopropyl group attached to the α-carbon?

Back 14

Valine

Front 15

Starting with Leucine, how do you get to isoleucine, structurally?

Back 15

Moving a methyl group form the gamma position to the beta position produces isoleucine.

Front 16

Which is the only Nonpolar, alipathic R group with sulfur?

Back 16

Met


Methionine

Front 17

List all the nonpolar, alipathic R groups.

Back 17

Glycine, Alanine, Proline, Valine, Leucine, Isoleucine, Methionine.

Front 18

List all the polar, alipathic R groups.

Back 18

Serine, Threonine, Cysteine, Asparagine, Glutamine.

Front 19

___ is like Alanine with a hydroxyl group at the beta-carbon.

Back 19

Ser


Serine

Front 20

Back 20

Ser


Serine

Hint 20

Polar, uncharged R group

Front 21

Back 21

Thr


Threonine

Hint 21

Polar, uncharged R group

Front 22

Back 22

Cys


Cystine

Hint 22

Polar, uncharged R group

Front 23

Back 23

Asn


Asparagine

Hint 23

Polar, uncharged R group

Front 24

Back 24

Gln


Glutamine

Hint 24

Polar, uncharged R group

Front 25

Back 25

Phe

F

Phenylalanine

Hint 25

Aromatic R Groups

Front 26

Back 26

Tyr


Tyrosine

Hint 26

Aromatic R group

Front 27

Back 27

Trp


Tryptophan

Hint 27

Aromatic R Group

Front 28

A hydroxylated phenylalanine yields which amino acid?

Back 28

Tyr


Tyrosine

Front 29

Which amino acid serves as a precursor to serotonin in the brain?

Back 29

Trp

Tryptophan

Front 30

When the enzyme that hydroxylates phenylalanine to tyrosine is not present and a buildup of phenylalanine happens, what illness can occur?

Back 30

Phenylketonuria

Front 31

What two amino acids are used to detect and measure proteins?

Back 31

Trp, Tyr @ 280nm


Tryptophan , Tyrosine

Front 32

Back 32

Lys


Lysine

Hint 32

Positively charged R group

(basic)

Front 33

Back 33

Arg


Arginine

Hint 33

Positively charged R group

(basic)

Front 34

Back 34

His


Histidine

Hint 34

Positively charged R group

(generally basic but can be weakly acidic depending on the environment)

Front 35

Back 35

Asp


Aspartate

Hint 35

Negatively charged R group

(acidic)

Front 36

Back 36

Glu

Glutamate

Hint 36

Negatively charged R group

(acidic)

Front 37

______ is a dimer of cysteine with a _________ linkage between the two monomers.

Back 37

Cystine ; disulfide

Front 38

List the amino acids that are essential (must be provided by diet).

Back 38

PVT TIM HALL

Phe, Val, Thr, Trp, Ile, Met, His, Arg, Lys, Leu

Front 39

Name the amino acids that contain sulfur.

Back 39

Front 40

True or False: There are some amino acids that occur in proteins but which are not included in the genetic code.

Back 40

True. These are synthesized by post-translational modification of precursor amino acids already incorporated into the proteins. Examples are...

[press "h" on your keyboard for the third side]

Hint 40

1. Hydroxyproline - Found in collagen. Formation requires vitamin C. [Vitamin C deficiency causes scurvy, a disease of connective tissue.]

2. γ-Carboxyglutamate - Formation requires vitamin K. Occurs in blood-clotting protein, prothrombin. [The anticoagulant drug, Coumadin (Dicoumarol) is a vitamin K antagonist.]

3. Selenocysteine - Plays a role in proteins involved in antioxidative mechanisms. [Selenium is an essential micronutrient but toxic in higher concentrations.]

Front 41

Amino acids are incorporated into proteins by forming _____ bonds with each other.

Back 41

Peptide bond , via a dehydration reaction.

Front 42

Amino acid residues joined together are considered a protein if...

Back 42

its molecular weight (MW) is greater than or equal to 10,000.

Front 43

A peptide is named from which terminus to which terminus?

Back 43

Amino terminus to carboxyl terminus.

Front 44

True or False: Peptide bonds characteristically have a trans configuration that has a double bond character.

Back 44

Hint 44

Due to resonance forms, the peptide bond has a signif degree of double bond character. This prevents rotation around the C-N bond, resulting in a rigid, planar structure. With a few important exceptions, peptide bonds are formed in the trans config.

Front 45

Which amino acids are considered basic due to the basic side chains?

(Carries positive charge at neutral pH.)

Back 45

His, Lys, Arg

Histidine, Lysine, Arginine