Chemistry and Metabolism of Amino Acids Flashcards

1
Q

General Structure of Alpha Amino Acid

A

acid (carboxyl group)
basic (amino group)
r group (distinct side chain)

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2
Q

Non-alpha AA present in tissues in free form

A

Beta alanine
Beta aminoisobutyrate
gamma aminoisobutyrate

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3
Q

Amino acid that is an IMINO ACID

A

Proline

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4
Q

Simple Amino Acid

A

Glycine

Alanine

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5
Q

Branched Chain AA

A

LIV

Lysine
Isoleucine
Valine

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6
Q

Sulfur Containing AA

A

Cysteine

Methionine

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7
Q

Hydroxyl Containing AA

A

Serine
Threonine
Tyrosine

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8
Q

AA w/ Amide Group

A

Asparagine

Glutamine

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9
Q

Acidic Amino Acid

A

Aspartate

Glutamate

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10
Q

Basic Amino Acid

A

Arginine - MOST BASIC
Lysine
Histidine

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11
Q

Aromatic AA

A

Histidine
Phenyalanine
Tyrosine - w/ OH group
Tryptophan

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12
Q

With heterocyclic Aromatic Ring

A

Tryptophan

Histidine - basic AA

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13
Q

Disrupts the alpha helix structure of proteins

A

PG

Proline
Glycine

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14
Q

SMALLEST SIDE CHAIN

A

Glycine

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15
Q

LARGEST SIDE CHAIN

A

Tryptophan

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16
Q

MOST BASIC AA

17
Q

MOST ACIDIC AA

A

Aspartic Acid

18
Q

Known as the 21st AA

A

SELENOCYSTEINE

19
Q

Known as the 22nd AA (found in Archaea)

A

PYRROLYSINE

20
Q

PURELY KETOGENIC AA

21
Q

BOTH Ketogenic and Glucogenic

A
Phenylalanine
Isoleucine
Tyrosine
Tryptophan
Lysine - predominantly ketogenic
22
Q

AA which absorb 250-290 nm UV light

A

Tryptophan
Phenylalanine
Tyrosine

23
Q

Formed from cytosine and uracil

A

Beta-Alanine

24
Q

MC amino acid that undergo oxidative deamination

A

Glutamic Acid (Glutamate)

25
General test for proteins Cupric ions in alkaline medium forms VIOLET color w/ peptide bond nitrogen
BIURET TEST - needs a minimum of 2 peptide bonds dipeptides and individual AA - do not answer biuret test
26
General test for all alpha amino acids
Ninhydrin Test AA + 2 mols of Ninhydrin --> aldehyde w/ 1 carbon atom less + CO2 + Purple Complex (Ruhemann's purple) AA which do NOT give purple color Proline and Hydroxyproline - YELLOW Glutamine and Asparagine - BROWN
27
Determined by the AA sequence of protein
Primary Structure N terminus to C terminus
28
The ONLY structure preserved in denaturation
Primary Structure
29
Folding of SEGMENTS of polypeptides Stabilized by hydrogen bonds
Secondary Structure alpha helix beta sheets
30
Alpha helix
Keratin | Hemoglobin
31
Beta sheets
Amyloid | Immunoglobulins
32
Overall 3D structure of of proteins Stabilized by disulfide bonds, hydrophobic interactions, hydrogen bonds and ionic interactions
Tertiary Structure
33
Interaction of atleast 2 peptide chains (tertiary structure)
Quaternary Structure