12.2 Proteins and Enzymes Flashcards

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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 tertiary structure important for?

A

Folding the peptide chain into a specific 3D structure

16
Q

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

A
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?

A
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
Q

What can denature proteins?

A

High temperature and change in pH

26
Q

How does temperature denature proteins?

A

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
Q

How does change in pH denature proteins?

A

It breaks the ionic bonds between the R groups in the tertiary structure

28
Q
A