Protein structure and enzymes (2.9–2.10) Flashcards

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1
Q

What is the basic structure of an amino acid?

A
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2
Q

How does a polypeptide chain form?

A

Amino acid monomers linked by peptide bonds in a condensation reaction.

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3
Q

What bonds are involved in a proteins primary structure?

A

Peptide bonds

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4
Q

What bonds are involved in the secondary structure of proteins?

A

Hydrogen bonds

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5
Q

What bonds are involved in the tertiary structure of proteins?

A
  1. Ionic bonds
  2. Disulphide bonds
  3. Hydrophobic and hydrophilic interactions
  4. Hydrogen bonds
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6
Q

What is the structure of globular proteins?

A

Round, compact proteins made up of multiple polypeptide chains.

Chains coiled up so hydrophobic are inside and hydrophilic are inside.

Soluble so easily transported in fluids.

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7
Q

What is the structure of fibrous proteins?

A

Fibrous protein’s are made up of long insoluble polypeptide chains that are tightly coiled to form a rope shape.

Lots of bonds so very strong

As strong often found in supportive tissue.

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8
Q

What is haemoglobin?

A

Globular protein made of 4 polypeptide chains. Carries oxygen around the body in the blood. It’s soluble, so can be easily transported. Iron containing haem groups that bind to oxygen.

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9
Q

What is collagen?

A

Strong, fibrous protein that forms connective tissue in animals.

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10
Q

What makes enzymes specific?

A

Active site which has a specific shape.

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11
Q

What are enzymes?

A

Biological catalysts that reduce activation energy.

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12
Q

How do enzymes reduce activation energy?

A

If two substrates need to be joined being attached to the enzyme joins them together, reducing the repulsion.

If causing a breakdown fitting into the active site puts a strain on bonds in the substrate so the substrate molecule breaks up more easily.

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13
Q

What are intracellular enzymes?

A

catalyse reactions inside cells

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14
Q

What are extracellular enzymes?

A

Produced and secreted by cell to catalyse reactions outside of cells.

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