Lesson 6: Proteins & Enzymes Flashcards

1
Q

What are proteins?

A

Macromolecules made of amino acid monomers

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2
Q

What are amino acids composed of?

A

-Amine group
-Central Carbon
-Hydrogen Atom
-R group
-Carboxyl group

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3
Q

What are peptides?

A

Polymers of 2 or more amino acids
- Dipeptides (2)
-Tripeptides (3)
-Oligopeptides (fevers than 10-15)
-Polypeptides (more than 15)
-Proteins (More then 100)

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4
Q

What is protein denaturation?

A

Drastic change that destroys the function of the protein (pH or heat)

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5
Q

What are the functions of proteins?

A

Structure: Collagen, Keratin (Helps Maintain hair, fingernails, and skin)
Communication: Some hormones, cell receptors
Membrane Transport: Forms channels, Carriers
Catalysis: Enzymes are catalysts that speed up rxns

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6
Q

What is an active site?

A

Indentation on an enzyme that fits with the substrate like a lock and key to create the enzyme-substrate complex.

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7
Q

True or False: Enzymes speed up the rate of reaction.

A

True

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8
Q

True or false: Enzymes are not reusable

A

False, they are reusable

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9
Q

True or False: Enzymes are specific to reactions and substrates

A

True

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10
Q

What is an allosteric site?

A

Sites that are distant from the active site
The activator binds to the allosteric site so that she shape changes and the active sites is available to the substrate
They allow us to absorb vitamins

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11
Q

What are inhibitors?

A

They stop the action by the enzyme (eg. poison and drugs)

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12
Q

What is a competitive inhibitor?

A

They bind to the active site to stop the substrate, blocking the substrate
-Possibly reversible by increasing the concentration of the substrate.

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13
Q

What is a non-competitive inhibitor?

A

Binds to the allosteric site and changes the shape of the active site.

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14
Q

What is an allosteric inhibitor?

A

It stabilizes the inactive form of the enzyme so that the substrate is released.

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15
Q

What are factors that affect enzyme activity?

A

-Cofactors (Metal ions)
-Coenzymes (Helper molecules needed for enzyme function)
-pH
-Temperature
-Concentration of substrates
-Concentration of enzymes (active sites available)

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16
Q

What is protein confirmation?

A

Overall 3D shape
Crucial function of proteins is to change their confirmation (eg. open and close membrane pores)

17
Q

What bond is created when peptides bond together?

A

Peptide bond (only time when you don’t need 2 hydroxides)

18
Q

How do amino acids act in solution?

A

Amino group bonds to an H+ ion, and the carboxyl group releases an H+ ion.