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Protein Structure

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Total cards: 24•Content version: v4•Public deck•Updated: 8/1/2026

Card preview (24)

#1
Front (Question)

The misfolding of what protein causes Alzheimers?

Back (Answer)

Amyloid B-peptide or Tau in the ER

#2
Front (Question)

The misfolding of which protein causes Parkinsons?

Back (Answer)

a-synuclein in the cytosol

#3
Front (Question)

The misfolding of which protein causes Cancer?

Back (Answer)

p53 in the cytosol

#4
Front (Question)

How many different amino acids are there?

Back (Answer)

20

#5
Front (Question)

What are the two major protein structures?

Back (Answer)

Alpha helix Beta sheet

#6
Front (Question)

How can the alpha helix be represented?

Back (Answer)

Backbone Sticks Ribbons Space filling

#7
Front (Question)

Where was the alpha helix first seen?

Back (Answer)

In the protein alpha keratin

#8
Front (Question)

Where do hydrogen bonds form in an alpha helix?

Back (Answer)

Between every forth peptide bond So on C=O is linked to a N-H

#9
Front (Question)

How often do alpha helixes have a complementary turn?

Back (Answer)

Every 3.6 amino acids

#10
Front (Question)

Where are alpha helixes abundant in the cell?

Back (Answer)

Cell membranes ie in transport proteins or receptors

#11
Front (Question)

Which amino acids do not favour helix forming?

Back (Answer)

Proline and Glycine

#12
Front (Question)

Beta Sheets can run in what two directions?

Back (Answer)

Parallel or anti-parallel

#13
Front (Question)

Which amino acids are usually found in the middle of the B sheets and why?

Back (Answer)

Aromatic residiues - Tyr, Phe, Trp, Val and Ile They are hydrophobic

#14
Front (Question)

What is always at the start of a protein?

Back (Answer)

The N terminus - NH2 COOH is always at the end

#15
Front (Question)

What are the four subunits of Src tyrosine kinase?

Back (Answer)

SH3 domain SH4 domain Small kinase domain Large kinase domain

#16
Front (Question)

In general, more complex organisms’ proteins have more what?

Back (Answer)

They have additional domains

#17
Front (Question)

What are the 3 types of non covalent weak bonds that can hold proteins together?

Back (Answer)

Hydrogen bonds Electrostatic attraction Van der Waals Attractions

#18
Front (Question)

Where do disulphide bonds form?

Back (Answer)

Inbetween two adjacent cysteine residues

#19
Front (Question)

Where do polar side chains tend to form in a folded protein?

Back (Answer)

On the outside of the folded protein so they can interact with water

#20
Front (Question)

The core of a folded protein can be known as what?

Back (Answer)

Hydrophobic

#21
Front (Question)

How can primary sequence be determined?

Back (Answer)

Inferred from DNA sequence Determined directly by amino acid sequencing using Edman degredation (chemical degredation) Mass Spectrometry (physical degredation)

#22
Front (Question)

What chemical does edman degredation use?

Back (Answer)

Phenylisothyocyanate (PITC)

#23
Front (Question)

Adding PITC to an amino acid chain forms what?

Back (Answer)

Phenylthiocarbamoyl derivative with the N terminus

#24
Front (Question)

What is formed when the N terminus is cleaved?

Back (Answer)

Cyclic compound of phenylthiohydantoin forms PTH amino acid This does not change the amino acid