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3.3.13.2 Proteins

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Total cards: 21•Content version: v4•Public deck•Updated: 8/1/2026

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#1
Front (Question)

What are the properties of polypeptides?

Back (Answer)

Strong and flexible

#2
Front (Question)

What does a peptide bond form between?

Back (Answer)

One of the hydrogen atoms of the amino group of one amino acid The OH group of the carboxylic acid of another amino acid

#3
Front (Question)

How do you hydrolyse proteins?

Back (Answer)

Boiling it in acid

#4
Front (Question)

Where do hydrophobic amino acid residues point?

Back (Answer)

Into the middle of the helix so that hydrophobic molecules can protect themselves

#5
Front (Question)

Where do hydrophilic amino acid residues point?

Back (Answer)

Out of the helix

#6
Front (Question)

What is the position of the residues in a beta pleated sheet?

Back (Answer)

They can point in any direction

#7
Front (Question)

Where are ionic bonds found in a DNA molecule?

Back (Answer)

Between charged residues

#8
Front (Question)

Where can van der Waals forces be found in a DNA molecule?

Back (Answer)

Between hydrophobic interactions

#9
Front (Question)

What is the process of thin layer chromatography?

Back (Answer)

The protein is hydrolysed by adding it to hydrochloric acid A small spot of amino acids is placed on a line 1cm above the bottom of the silica plate The plate is placed in a solvent where the solvent does not reach the line The solvent is called the mobile phase The solvent rises up the plate, carrying the amino acids with it The amino acids which lag behind have a lower affinity for the solvent due to the decreased intermolecular forces The solvent front is the line reached by the solvent When the solvent has reached far up the plate, the plate is removed and the points reached by the amino acids is marked The plate is marked by spraying it with ninhydrin then shining ultra-violet light on it Rf = distance moved by spot / distance moved by solvent The Rf value is the same for every amino acid

#10
Front (Question)

What are proteins?

Back (Answer)

Sequences of amino acids joined by peptide bonds

#11
Front (Question)

How is a polypeptide formed?

Back (Answer)

OH of the carboxylic acid H of the amine group Forms a CONH group

#12
Front (Question)

How do you work out the monomer of a condensation polymer?

Back (Answer)

Find the linkage group

#13
Front (Question)

Why are polyethene and polypropene bad for the environment?

Back (Answer)

They’re long chain alkene molecules so are unreactive and are not biodegradable

#14
Front (Question)

What functional groups does an amino acid have?

Back (Answer)

Amine and carboxylic acid

#15
Front (Question)

How many naturally occuring amino acids are there?

Back (Answer)

20

#16
Front (Question)

What are the properties of an amino acid?

Back (Answer)

Chiral: four different functional groups Ionic: dissolve in water

#17
Front (Question)

Functional group of an amide?

Back (Answer)

-CONH2

#18
Front (Question)

What type of polymer is a polypeptide?

Back (Answer)

Condensation polymers because water is formed when the amino acid acids join

#19
Front (Question)

How do you hydrolyse proteins?

Back (Answer)

Boil in HCl which hydrolyses the peptide linkages

#20
Front (Question)

What are the types of bonds that hold a protein together?

Back (Answer)

Hydrogen bonding Ionic attractions Disulfide bridges: -CH2S - SCH2-

#21
Front (Question)

How can amino acids be seperated?

Back (Answer)

Thin layer chromatography Plate consisting of a thin, flexible layer of silica The white powder is the stationary phase A small spot is placed at the bottom of the paper The end of the plate is placed in a solvent The solvent rises up the plate, carrying the amino acids The stronger the intermolecular forces between the amino acid and the solvent, the closer the amino acid is to the solvent front