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Flashcards in Amino Acids Deck (35):
1

The alpha carbon is chiral in all molecules except _____

glycine

2

All amino acids found in natural proteins are ______amino acids

L-amino acids (with a few exceptions)

3

A zwitterion amino acid exist in ____state and has no overall _____but have parts of positive and negative charges

solid state; net charge

4

____ amino acids are used directly in the processes of protein synthesis

Standard

5

____amino acids are modified after the protein is completed or used in other cellular processes (such as the urea cycle)

Non standard

6

Single amino acids within a protein often are referred to as amino acid ______

residues

7

What are essential amino acids

Amino acids acquired through diet

8

What are the essential amino acids

1. Histidine
2. Isoleucine
3. Leucine
4. Lysine
5. Methionine
6. Phenylalanine
7. Threonine
8. Tryptophan
9. Valine

9

What are conditionally non essential amino acids

required at some stages of growth or by some people who cannot synthesize them, either because of genetics or a medical condition

10

What are the conditionally non essential amino acids

1. Arginine
2. Asparagine
3. Glutamine
4. Glycine
5. Proline
6. Serine
7. Tyrosine

11

what are the non essential amino acids

1. Alanine
2. Aspartate
3. Cysteine
4. Glutamate

12

What are the nonpolar, aliphatic amino acids

1. Alanine (Ala, A)
2.Glycine (Gly, G)
3. Isoleucine (Ile, I)
4. Leucine (Leu, L)
5. Methionine (Met, M)
6. Proline (Pro, P)
7. Valine (Val, V)

13

What are non polar, aliphatic amino acids important for

hydrophobic protein interactions.

14

Gly allows structural flexibility due to its small ____

size

15

Pro reduces flexiblity because of its ___amino group structure

secondary. Its rigid and distrupts protein folding structures. It connects beta strands

16

What is considered a copper trafficking protein

methionine

17

What are the polar, uncharged amino acids

1. Cysteine (Cys, C)
2. Asparagine (Asn, N)
3. Glutamine (Gln, Q)
4. Serine (Ser, S)
5. Threonine (Thr, T)

18

What is the polarity due to in the polar, uncharged amino acids

1. OH groups (Ser, Thr)
2. S atom (Cys)
3. amide groups (Asn, Gln)

19

The -OH sites of serine and threonine are sites for _____ modifications

covalent

20

Cysteine forms covalent disulfide bonds important for _____folding

protein

21

Asparagine and Glutamine are important ______donors/carriers

Nitrogen

22

Hydrogen bonds stabilize the _____ structure

secondary. Found in alpha helices and beta sheets

23

What are the aromatic amino acids

1. Phenylalaline (Phe, F)
2. Tyrosine (Tyr, Y)
3. Tryptophan (Trp, W)

24

Aromatic amino acids are relatively ______polar so they can participate in _____interactions.

nonpolar; hydrophobic

25

A catecholamine is a naturally occurring amine that is ______and functions as neurotransmitter and ____

aromatic; hormones

26

Tyrosine-->DOPA-->Dopamine-->Norephinephrine-->_____

Epinephrine

27

What are some positively charged (basic) amino acids

1. Arginine (Arg, R)
2. Histidine (His, H)
3. Lysine (Lys, K)

28

What are some negatively charged (acidic) amino acids

1. Aspartate (Asp, D)
2. Glutamate (Glu, E)

29

Why are they negatively charged?

Carboxyl group (COO-) side chain

30

What do the negatively charged acidic amino acids participate in

in the formation of salt bridges and stabilize the tertiary structure

31

what are the nonstandard amino acids

1. 4-hydroxyproline:
2. 5-hydroxylysine: both collagen
3. N- methyllysine: myosin
4. y-carboxyglutamate: Prothrombin
5. Desmosine: Elastin

32

Non standard amino acids are _____after the protein is synthesized

modified

33

What are collagen specific amino acids

Important in cross linking of fibrils

34

What is ascorbate a cofactor for

prolyl hyroxylase

35

What is demosine made of

4 lysine residues; contributes to stretchiness of elastin