Flashcards in Amino Acids Deck (35)
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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
