Proteins Flashcards

1
Q

What is the function of the protein?

A
  • Give you your structure
  • Hold body together
  • Direct metabolic functions
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2
Q

Are proteins monomers or polymers?

A

Polymers

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3
Q

What is the monomer of the protein?

A

Amino acid

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4
Q

How many sets of amino acids do living things have?

A

20

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5
Q

What is the basic structure of the amino acid?

A
  • central carbon with 4 functional groups
    1. amino group (H2N)
    2. carboxyl group
    3. hydrogen
    4. “R” variable group
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6
Q

What does the R group determine?

A
  1. Identity of amino acid
  2. Physical properties (size and shape)
  3. Chemical properties (polarity, pH level)
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7
Q

Define ligament

A

Connect bone to bone

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8
Q

Define tendons

A

Connect muscle to bone

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9
Q

What are protein markers?

A

Proteins in the cell that mark your cells as being yours

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10
Q

What charges do amino acids have?

A

They can be non-polar, polar, or charged

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11
Q

What is the function of enzymes?

A

Proteins act as enzymes which are catalysts to speed up chemical reactions

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12
Q

What is the function of structural support?

A

Ligaments and tendons allow you to stand. These proteins give your body its structure.

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13
Q

What is the function of motile?

A

Proteins will allow you to move- muscles will contract and move parts of your body

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14
Q

What is the function of carriers? An example?

A

Proteins will carry or transport materials throughout the body. Ex. Hemoglobin to carry O2

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15
Q

What is the function of recognition?

A

Special proteins markers occur on all of your cells which tell the immune system that the cell is yours and belongs

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16
Q

What is the function of defensive proteins?

A

Proteins called antibodies will recognize and attack foreign invaders such as viruses or bacteria

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17
Q

What is the polymer of proteins?

A

Polypeptide

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18
Q

Define a polypeptide chain?

A

Linear chain composed of amino acids covalently bonded to each other

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19
Q

What is the condensation reaction in proteins

A

Removal of water molecule as two amino acids are joined

20
Q

Where does the bond take place in the amino acid?

A

Between the amino group of one acid and the carboxylic group of the other

21
Q

Define a peptide bond

A

Covalent bond between amino acids

- bond between primary structure

22
Q

What determines the function of a protein?

A

The sequence of amino acids

23
Q

What happens when there is failure to achieve the proper conformation?

A

Non- functioning protein

24
Q

How many levels/ structures does a protein have?

A

4

25
Q

What is the conformation of proteins a result of?

A

Structural levels of protein and sequence of amino acids

26
Q

What is the primary level of a protein?

A

The specific sequence of amino acids joined together

- determined by gene in protein

27
Q

What are on the ends of a primary structure?

A

Amino group and carboxylic acid

28
Q

What does the sequence of the primary structure determine?

A

How the secondary and tertiary levels form

29
Q

What is the secondary level/ structure?

A

Defined as the way the polypeptide chain is coiled and folded upon itself

30
Q

What are the two types of secondary structures?

A

Alpha helix and beta pleated sheet

31
Q

What are protein conformations held by in a secondary structure?

A

Hydrogen bonds

32
Q

What are the secondary structures dependent on?

A

The amino acid in the section

33
Q

Define an alpha helix

A
  • Polypeptide chain is coiled
  • Hydrogen bonds between every 4th amino acid
  • Found in hair and horns
34
Q

Define a beta plated sheet

A
  • chain folded back with regions of chain parallel to itself

- found in spider silk

35
Q

Define the tertiary level

A

The overall 3D structure of a polypeptide.

36
Q

What creates a fold?

A

R groups from 2 amino acids bonding

37
Q

What are the forces holding tertiary conformation?

A
  1. hydrogen bonds
  2. ionic bonds
  3. hydrophobic interactions (of two nonpolar R groups will clump)
  4. Disulfide bonds
38
Q

Define the quaternary level/ structure

A

Found only in proteins with more than one polypeptide chain

- not all proteins have them

39
Q

Define denaturation

A

Loss of conformation

- unfolding of tertiary and secondary structures

40
Q

What happens when a protein is denatured?

A

It becomes non- functional

41
Q

What causes denaturation in protein?

A
  1. high temperature
  2. pH that is too high or too low
  3. high salt concentration
  4. solvent (ex. alchohol)
42
Q

What happens if you destroy the primary structure of the protein?

A

The protein is destroyed

43
Q

Define polypeptide

A

Strand of 3+ amino acids

44
Q

How does a protein differ from a polypeptide?

A

A protein can contain more than one polypeptide and takes on 3D shapes

45
Q

What gives proteins acidic properties?

A

The carboxyl group attached

46
Q

Where does a peptide bond form?

A

Between the carboxyl group of one amino acid and the amino group of another through dehydration synthesis

  • OH removed from carboxyl group
  • H removed from amino group
  • bond formed between carbon and nitrogen
47
Q

What is the tertiary structure due to?

A

Primarily due to the interactions between the R groups of the amino acids that make up the protein.