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Molecules to Cells - Biochemistry > Lecture 7. Proteins > Flashcards

Lecture 7. Proteins Flashcards

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Organic Chemistry 101 flashcards
1
Q

What does a peptide bond do ?

A

Connects amino acids

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2
Q

What direction are hydrogen bonds ?

A

Diagonal

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3
Q

Do outward facing side chains play a part in hydrogen bonding ?

A

No

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4
Q

What is dihydrofolate reductase ?

A

An enzyme that reduces dihydrofolate to tetrahydrofolate

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5
Q

What is the coenzyme of dihydrofolate reductase ?

A

NADPH

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6
Q

What does dihydrofolate reductase do ?

A

Important in one carbon metabolism and synthesis of nucleic acid

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7
Q

What are super helixes ?

A

Two right handed alpha helix intertwined with the presence of a disulphide bridge

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8
Q

What is collagen the main component of ?

A

Skin, bone, tendon, cartilage and teeth

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9
Q

What is the structure of collagen ?

A
  1. Rod shaped
  2. 3000 A long, 15 A diameter
  3. Three left-handed helical 1000 residue polypeptide chains
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10
Q

What is the third amino acid in collagen

A

Glycine

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11
Q

What is the frequent repeat seen in collagen ?

A

Glycine, proline and 4-hydroxyproline

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12
Q

Discuss a quality control measure taken if a protein is still in the cell

A

Protosomes and other molecules can degrade the protein into amino acids and try again

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13
Q

What happens if a protein is folded incorrectly outside the cell ?

A

It may still function or it may aggregate to amyloid fibrils

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14
Q

What is alzheimers caused by ?

A

The amyloid fibrils in brain kills cells

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15
Q

What is parkinsons caused by ?

A

Aggregation of alpha synuclein

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16
Q

What is needed for a protein to unfold ?

A
  1. Ribonuclease A to unfold
  2. Addition of a chemical denaturant
  3. Reducing agent added to break disulphide bridges
17
Q

What contains all the information for the protein to fold ?

A

The amino acid polypeptide chain

18
Q

Do we observe step wise, gradual folding en-route to the native state ?

A

No we see hydrophobic collapse and slow reorganisation of side chains to attain native structure

19
Q

Thermodynamically, what is the native structure at ?

A

Global free energy minimum

20
Q

What do molecular chaperones or chaperonins do ?

A

Assist protein folding

21
Q

What is an assay ?

A

A track protein

22
Q

What must be used to purify proteins ?

A

an assay

23
Q

What is isoelectric focusing ?

A

Protein separation based on pI

Molecules to Cells - Biochemistry (17 decks)

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