Peptides and Proteins Flashcards

1
Q

What type of bonds are planar?

A

peptide bonds

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2
Q

Where do 20 different possible side chains protrude from?

A

the repeating backbone of a protein

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3
Q

What are the bonds listed from strongest to weakest?

A

ionic-> covalent-> disulfide-> salt-> hydrogen-> electrostatic-> Van der Waals

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4
Q

What are the characteristics of a primary structure?

A
  • sequence of covalent bonds
  • very stable
  • amino acid sequence contains info. required for protein building
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5
Q

What structure determines the folded structure of a protein?

A

primary structure

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6
Q

What are the characteristics of the secondary structure?

A
  • reverse turn (beta turn)
  • alpha-helix
  • alpha-helical interactions
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7
Q

What bonds are associated with each structure?

A
  • covalent-> primary & tertiary
  • hydrogen-> secondary
  • noncovalent interaction-> quarternary
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8
Q

In a beta strand of a secondary structure, where are the side chains located?

A

above and below the plane strand

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9
Q

What is the difference between a parallel and antiparallel beta sheet?

A
  • parallel: strands run in the SAME direction; H bonds connect an amino acid to 2 amino acids on adjacent strand (1:2 bond)
  • antiparallel: strands run in OPPOSITE direction; H bonds connect 1 amino acid to 1 amino acid on adjacent strand (1:1 bond)
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10
Q

Which beta sheet stabilizes the secondary structure?

A

antiparallel

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11
Q

Myoglobin/aquaporins have what on the inside and what on the outside?

A

hydrophilic on the inside and hydrophobic on the outside

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12
Q

Myoglobin is in what structure?

A

tertiary

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13
Q

In the tertiary structure of a protein, where are the hydrophobic and charged (hydrophilic) amino acids found?

A

hydrophobic are found on the inside and charged are found on protein surface

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14
Q

What is the role of beta-mercaptoethanol in denaturation?

A

responsible for reducing disulfide bonds

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15
Q

What is the role of urea in denaturation?

A

breaks down H bonds, Van der Waals, and salt bridges

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16
Q

What 2 amino acids absorb at 280 nm because of aromaticity?

A

trp & tyr

17
Q

How is Edman degradation used for studying primary structure?

A
  • used for short polypeptides
  • cleaves amino acids one at a time
  • N-terminus removed
18
Q

How is protease specificity used for studying primary structure?

A
  • used for long polypeptides
  • cleaves at COOH end
19
Q

In protease specificity, what does each amino acid cleave?

A
  • trypsin: arg & lys on COOH side
  • chymotrypsin: phe, tyr, trp
  • CNBR: met
20
Q

What are the methods of studying each protein structure?

A
  • primary-> mass spectroscopy
  • secondary-> circular dichroism spectroscopy
  • tertiary-> X-ray crystallography
21
Q

What structures are able to be denatured?

A

secondary, tertiary, quarternary