Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Chemistry Module 2 > Amino acids > Flashcards

Amino acids Flashcards

You may prefer our related Brainscape-certified flashcards:
Periodic Table flashcards Chemistry 101 flashcards AP® Chemistry flashcards Organic Chemistry 101 flashcards
1
Q

What do amino acids contain

A

They contain a COOH group and an NH2 group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is special about an α (alpha) amino acid?

A

They have an NH2 and COOH group bonded to the same carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Draw an amino acid with an R group

A

on page

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are the equilibrium equations with H+ ions

A
  1. NH2 + H+ → NH3

2. COOH → COO- + H+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What happens to the equilibrium in acidic and alkaline solutions?

A

on page

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Draw an amino acids in acidic, alkaline solutions

Draw a zwitterion

A

on page

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What are all amino acids at a low pH

A

All NH2 groups are pronated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are all amino acids at a high pH

A

All COOH groups are depronated in high pH solutions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Draw lysine at pH 7 and pH 1

A

on page

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Draw the structure of glycine, alanine, lysine and glutamic acid

A

On page

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are some physical properties of amino acids?

A
  1. High melting points
  2. Exist as dipolar ions, attraction between them is very strong
  3. Soluble in water
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Give an example of the reaction of Glycine with sodium carbonate and where do these reactions take place on the molecule?
Observations?

A

2H2NCH2COOH + Na2CO3 → 2H2NCH2COONa + CO2 +H2O

Occur at the COOH group.
Bubbles of gas produced

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Give an example of the reaction of Glycine with nitrous acid.
How is the nitrous acid formed? Where does the reaction occur? Observations

A

Nitrous acid is formed in situ from Sodium nitrite and Hydrochloric acid (HNO2)
The NH2 group is replaced by OH group
H2NCH2COOH + HNO2 →HOCH2COOH + N2 + H2O
Bubbles of gas produced

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Give an example of the reaction of glycine with copper (II) sulfate. What is formed? What does glycine act as?
Observations

A

A complex is formed with a coordination number of 4.
Glycine acts as a bidentate ligand

Cu2+ + 2H2NCH2COOH → [Cu(H2NCH2COOH)2]2+

Blue solution formed when solutions of copper (II) sulfate and glycine are mixed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

How are peptides formed?

A

Amino acids react together in a condensation polymerisation to form peptides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is the peptide group?

A

-CONH-

17
Q

Show the formation of a peptide from glycine and alanine

A

on page

18
Q

What are the two ways a peptide link can be hydrolyses?

A

Acidic - All NH2 groups become pronated to NH3+, COOH remains untouched. Positive amino acids
Alkaline - The amino acid formed is depronated, all COOH become COO-, negative amino acids. NH2 unaffected

19
Q

How are amino acids identified?

A

All are colourless, chromatography is used, sprayed with ninhydrin and the compared against known Rf values.

20
Q

What is the primary structure?

A

Sequence of amino acids joined by peptide links in the chain

21
Q

What is secondary structure?

A

The twisting/coiling of the chain to form a β pleated sheet /α helix by intramolecular hydrogen bonding

22
Q

What is tertiary structure?

A

The bending/folding of the secondary structure to give a precise 3D shape held together by hydrogen bonding / disulphide brides / ionic interactions / Van der Waals

23
Q

What causes the different interactions?

A

The R groups are generally responsible for the interactions of amino acids. Non polar R groups are hydrophobic

24
Q

Give a description of proteins as enzymes

A

Enzymes are biological catalysts. Enzymes provide an active site, the substrate binds to the active site. Initially binding holds it, but then changes occur in the active to fit around the substrate and hold it strongly. Induced fit model . Chemical groups in the active site catalyse the reaction.

25
Q

What happens to enzymes at higher temperatures and non optimal pH

A

Temp - The enzyme become denatured, the bonds which hold the tertiary shape together are broken
pH - If the equilibrium of NH2 and COOH is altered it will affect the bonding

26
Q

What are the different enzymes for carbohydrates, lipids and proteins?

A

Carbs - Amylase
Protein - Protease
Lipids - Lipase

27
Q

What benefits are there of enzymes in washing powder?

A

Function at a lower temperature therefore save money

Chemistry Module 2 (13 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions