12.2 Proteins and Enzymes Flashcards

(29 cards)

1
Q

What elements do all amino acids contain?

A

Nitrogen, carbon, hydrogen and oxygen

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2
Q

What do some proteins contain?

A

Sulphur

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3
Q

What do each protein have?

A

A specific shape and therefore a specific function

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4
Q

What bonds are found in proteins?

A

Peptide bonds

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5
Q

What monomers make up proteins?

A

Amino acids

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6
Q

What is the general structure of an amino acid?

A

It has a central carbon atom, to which nitrogen containing an amine group and carboxyl group are attached. The different R group is what makes amino acids different.

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7
Q

R groups can be…

A

Positively charged, Negatively charged, Hydrophilic or Hydrophobic

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8
Q

What is a dipeptide?

A

A dimer made by two amino acids joined together by a condensation reaction (forming a peptide bond)

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9
Q

What are the four protein structures?

A

Primary structure
Secondary structure
Tertiary structure
Quaternary structure

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10
Q

Describe the primary structure

A
  • it is the number and sequence of amino acids in a polypeptide chain
  • it ONLY involves peptide bonds
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11
Q

What is the primary structure responsible for?

A

The overall structure of protein - changing one amino acid may alter the structure and function of the protein

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12
Q

What does the primary structure look like?

A
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13
Q

What do polypeptide chains fold into? (secondary structure)

A

Alpha helices and Beta pleated sheets

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14
Q

What bonds are found in secondary structure?

A

Weak hydrogen bonds

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15
Q

Why are secondary structures stable and strong?

A

They contain many hydrogen bonds which provide strength in numbers

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16
Q

What is the structure of an Alpha Helix and a Beta Pleated Sheet?

17
Q

What does the R group do?

A

It determines the different shapes of proteins

18
Q

What bonds are found in the tertiary structure?

A

Weak hydrogen bonds, ionic bonds and disulphide bridges

19
Q

Why is the tertiary structure important?

A

It determines how the protein will interact with other molecules

20
Q

Describe the quaternary structure?

A

Two or more polypeptide chains joined together

21
Q

What is the tertiary structure of a protein?

22
Q

What are the two types of quaternary structures?

A

Globular (functional) and Fibrous (structural)

23
Q

Describe a globular protein

A
  • It is either tertiary or quaternary
  • Compact and folded into spherical molecules
  • Soluble in water
24
Q

Describe a fibrous protein

A
  • Made from a-helices twisting around each other
  • Chains have cross linkages (mainly Hydrogen bonds) forming long strands
  • Strong, tough and insoluble
25
What can denature proteins?
High temperature and change in pH
26
How does temperature denature proteins?
Increasing temperature increases the kinetic energy of molecules, therefore causing more vibrations. These vibrations can break the weak hydrogen bonds in the secondary and tertiary structure - changing the overall shape of the protein
27
How does change in pH denature proteins?
It breaks the ionic bonds between the R groups in the tertiary structure
28
29
What is the tertiary structure important for?
Folding the peptide chain into a specific 3D structure