Chapter 2 : Proteins Flashcards

(35 cards)

1
Q

What are proteins

A

A molecule composed of amino acids joined together by peptide bonds

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2
Q

How many amino acids are there in total

A

20

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3
Q

What is the basic monomer of proteins

A

amino acids

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4
Q

What are the three major groups of an amino acid ?

A

amino group (NH2) , carboxyl group ( COOH) and the side chain

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5
Q

What group gives the identity of the amino acid

A

the side chain

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6
Q

What kind of shape do amino acids have ?

A

tetrahedral shape

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7
Q

True or false , the central carbon on an amino acid is not chiral

A

False , the central carbon is chiral

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8
Q

What are the two enantiomers of all amino acids ?

A

L and D

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9
Q

Between the L and the D isomer, which one is mostly found in proteins

A

The L isomer

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10
Q

How many different types of amino acids are there?

A

5

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11
Q

Non-polar Aliphatic Amino acids

A
  • Nonpolar
  • Water insoluble ( CH bonds)
  • 7 amino acids
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12
Q

Aromatic Amino Acids

A
  • Contain an aromatic group
  • nonpolar
  • Able to absorb UV light
  • 2 amino acids
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13
Q

Polar Uncharged Amino Acids

A
  • Contain polar bonds ( OH, SH, or NH)
  • contain no charges
  • more soluble in water
  • 6 amino acids
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14
Q

Acidic Amino Acids

A
  • side chain is a COOH group
  • weak acids but exist as COO- at neutral pH
  • 2 amino acids
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15
Q

Basic Amino Acids

A
  • Contain net positive charges at neutral pH
  • contain amine group as side chain which is protonated
  • 3 amino acids
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16
Q

How many dissociable hydrogens does every amino acid have AT LEAST ?

17
Q

pK1

A

1/2 of the amino acid molecules have lost H from the COOH

- falls between pH of 2.0-2.4

18
Q

pK2

A

1/2 of amino acid molecules have lost H+ from NH3 group

- falls between pH of 9.0-9.8

19
Q

Where do peptide bonds form?

A

Between the carboxyl group of the 1st aa and the amine group of the 2nd amine

20
Q

What is a biproduct of a peptide bond

A

water, dehydration synthesis

21
Q

True or False, the peptide bond is a single bond which has resonance form in a double bond

A

True, the double bond inhibits rotation creating stability and polarity in the protein backbone

22
Q

How many levels of protein structure are there ?

23
Q

Primary structure

A

sequence of amino acids

24
Q

Secondary structure

A

hydrogen bonding between adjacent amino acids to create α-helix or β-pleated sheet

25
Teritary structure
complete 3D shape of the polypeptide chain
26
Quarternary structure
structure that results after two or more interacting polypeptide chains come together
27
True or false, the primary structure contains all the info for the final 3D shape
True
28
True or false, the backbone of the protein is 3D
False, the backbone of a protein is planar
29
α-Helix
- found in secondary structure - All H bonds are parallel to the axis - helices can be right or left handed
30
β –pleated sheet
- formed from the protein backbone - can either be parallel or antiparallel - side chains extend out perpendicularly
31
β-turn
When the β-sheet is formed , the turn allows fo the backbone to bend, turn or reorient
32
Hydrophobic protein interactions
Nonpolar side chains cluster to avoid interaction resulting in protein folding
33
Ionic protein interactions
Attractions or repulsions between opposite or like charges on the side chains
34
Van Der Waal protein interactions
- quick dipole-dipole reactions resulting in fluctuations in electron distribution
35
Denaturation
the process which protein function begins to degrade due to the surrouding eniorment