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Flashcards in Amino Acids Deck (35)
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1
Q

The alpha carbon is chiral in all molecules except _____

A

glycine

2
Q

All amino acids found in natural proteins are ______amino acids

A

L-amino acids (with a few exceptions)

3
Q

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

A

solid state; net charge

4
Q

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

A

Standard

5
Q

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

A

Non standard

6
Q

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

A

residues

7
Q

What are essential amino acids

A

Amino acids acquired through diet

8
Q

What are the essential amino acids

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

What are conditionally non essential amino acids

A

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

10
Q

What are the conditionally non essential amino acids

A
  1. Arginine
  2. Asparagine
  3. Glutamine
  4. Glycine
  5. Proline
  6. Serine
  7. Tyrosine
11
Q

what are the non essential amino acids

A
  1. Alanine
  2. Aspartate
  3. Cysteine
  4. Glutamate
12
Q

What are the nonpolar, aliphatic amino acids

A
  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
Q

What are non polar, aliphatic amino acids important for

A

hydrophobic protein interactions.

14
Q

Gly allows structural flexibility due to its small ____

A

size

15
Q

Pro reduces flexiblity because of its ___amino group structure

A

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

16
Q

What is considered a copper trafficking protein

A

methionine

17
Q

What are the polar, uncharged amino acids

A
  1. Cysteine (Cys, C)
  2. Asparagine (Asn, N)
  3. Glutamine (Gln, Q)
  4. Serine (Ser, S)
  5. Threonine (Thr, T)
18
Q

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

A
  1. OH groups (Ser, Thr)
  2. S atom (Cys)
  3. amide groups (Asn, Gln)
19
Q

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

A

covalent

20
Q

Cysteine forms covalent disulfide bonds important for _____folding

A

protein

21
Q

Asparagine and Glutamine are important ______donors/carriers

A

Nitrogen

22
Q

Hydrogen bonds stabilize the _____ structure

A

secondary. Found in alpha helices and beta sheets

23
Q

What are the aromatic amino acids

A
  1. Phenylalaline (Phe, F)
  2. Tyrosine (Tyr, Y)
  3. Tryptophan (Trp, W)
24
Q

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

A

nonpolar; hydrophobic

25
Q

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

A

aromatic; hormones

26
Q

Tyrosine–>DOPA–>Dopamine–>Norephinephrine–>_____

A

Epinephrine

27
Q

What are some positively charged (basic) amino acids

A
  1. Arginine (Arg, R)
  2. Histidine (His, H)
  3. Lysine (Lys, K)
28
Q

What are some negatively charged (acidic) amino acids

A
  1. Aspartate (Asp, D)

2. Glutamate (Glu, E)

29
Q

Why are they negatively charged?

A

Carboxyl group (COO-) side chain

30
Q

What do the negatively charged acidic amino acids participate in

A

in the formation of salt bridges and stabilize the tertiary structure

31
Q

what are the nonstandard amino acids

A
  1. 4-hydroxyproline:
  2. 5-hydroxylysine: both collagen
  3. N- methyllysine: myosin
  4. y-carboxyglutamate: Prothrombin
  5. Desmosine: Elastin
32
Q

Non standard amino acids are _____after the protein is synthesized

A

modified

33
Q

What are collagen specific amino acids

A

Important in cross linking of fibrils

34
Q

What is ascorbate a cofactor for

A

prolyl hyroxylase

35
Q

What is demosine made of

A

4 lysine residues; contributes to stretchiness of elastin