Amino Acids Flashcards

(33 cards)

1
Q

Amino Acid Groups

A

NH2 and COOH
alpha aa has NH2 and COOH bonded to same carbon

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2
Q

Amino Acid Structure

A
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3
Q

Amino Acid if R group is H

A

Glycine

Not Optically Active

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4
Q

Amino Acid if R group is CH3

A

Alanine

Optically Active - most aa are

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5
Q

Two Groups in Equilibrium w/ H+ Ions

A
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6
Q

Equilibria in Acidic Solution

A

A is pushed RHS
B is pushed LHS

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7
Q

Amino Acid In Low pH

A
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8
Q

Equilibria in Alkaline Solution

A

A is pushed LHS
B is pushed RHS

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9
Q

Amino Acid in high pH

A
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10
Q

Zwitterion

A

have a permanent positive and negative charge, but are neutral overall

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11
Q

Isoelectric Point

A

Certain pH amino acid exists as a dipolar zwitterion

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12
Q

Structure and IUPAC
Glycine

A

Aminoethanoic Acid

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13
Q

Structure and IUPAC
Alanine

A

2-aminopropanoic acid

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14
Q

Structure and IUPAC
Lysine

A

2,6-diaminohexanoic acid

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15
Q

Structure and IUPAC
Glutamic Acid

A

2-aminopentanedioic acid

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16
Q

Physical Properties Amino Acids

A

•high mp
-exist as dipolar ions - attraction between is strong

•soluble in water
-dipolar ions can interact with polar water molecules

17
Q

Amino Acid w/ Sodium Carbonate

A

Reactions occur at COOH

Obsv: bubbles of colourless gas(CO2)

18
Q

Amino Acids w/ Nitrous Acid

A

HNO2 formed in situ from sodium nitrite and HCl

NH2 replaced by OH

Obsv: bubbles colourless gas (N2)

19
Q

Glycine w/ Copper(II) Sulfate

A

Complex formed with coord number 4

Glycine acts as bidentate ligand

Obs: blue solutions formed on mixing

20
Q

Formation of Peptides

A

Amino acids react together in condensation reaction to form peptides

21
Q

Acid Hydrolysis of a Peptide

A

Amino acids formed are protonated - all NH2 become NH3+

Positive amino acid ions

COOH stay as COOH

22
Q

Alkaline Hydrolysis of Peptide

A

Amino acids are deprotonated - all COOH become COO-

Negative amino acid ions

NH2 stay as NH2

23
Q

How may Amino Acids prod in Hydrolysis be seperated and identified

A

Thin-Layer Chromatography

Colourless so Ninhydrin stain used to locate position of spot

Rf used to identify amino acids

24
Q

Primary Protein

A

Sequence of amino acids joined by peptide links in a chain

25
Secondary Protein
twisted/coiled ß-pleated sheet/a-helix which is formed and held together by intramolecular hydrogen bonding
26
Tertiary Protein
bending/folding of the secondary structure to give a precise 3D shape which is held together by H bonding/disulfide bridges/ionic interactions/van der Waals forces
27
Enzyme
Protein that is a biological catalyst
28
Active Site
Site on surface of the enzyme into which its substrate fits
29
Induced Fit Model
involves the substrate inducing a change in the shape of the active site of the enzyme
30
Enzymes Stereospecific
Only one optical isomer of a substrate will fit into active site
31
Enzyme Function Temp Dependant
Optimum temp in which function is at maximum Higher temp = denatured - coiling and folding break down Peptide bonds do not break above opt temp
32
Enzymes Optimum pH
Enzyme denatures when pH altered due to equilibrium of NH2 and COOH group alters - changing bonding Peptide bonds not broken
33
Enzymes in Biological Washing Powders/Liquids
Added to break down biological molecules in stains - trad detergents without enzymes may not be able to remove stains of blood and fatty food stains **Protease** added to breakdown protein stains **Amylase** break down carb **Lipase** break down fats, hudrolysis Allows washing powders to function at lower temp - more cost effective