Proteins And Enzymes Flashcards

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1
Q

Proteins are also?

A

Polymers

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2
Q

Amino acids are also called?

A

Monomers

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3
Q

What are Amino acids?

A

A carbon bound to a amino group, carboxyl group, hydrogen and a side chain (or R group)

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4
Q

What group is different in each amino acid?

A

R group (side chain)

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5
Q

What is the structure of amino acids?

A

H = O
H — N — C — C — OH
. R group

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6
Q

What is a Peptide bond?

A

The bond between the carboxyl group of one amino acid to the amino group of another amino acid.

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7
Q

How to form a protein?

A

Amino acids binding to other amino acids; each creating a peptide bond with the next amino acid

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8
Q

What is a peptide?

A

Any molecule with a peptide bond

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9
Q

What is a polypeptide?

A

2-49 amino acids

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10
Q

What is a protein?

A

50+ amino acids

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11
Q

How many structures can a protein have and what are they?

A

There is 4.
Primary structure
Secondary structure
Tertiary structure
Quaternary structure

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12
Q

What is primary structure?

A

The order and number of amino acids

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13
Q

What is secondary structure?

A

The folding of chain into β-pleated sheets or α-helices

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14
Q

What is a β-pleated sheet?

A

Folded structure

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15
Q

What is α-helices?

A

Twisted, curled structure

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16
Q

What is Tertiary structure?

A

Folding of both α-helices and β-pleated sheets into a 3D structure

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17
Q

What is a quaternary structure?

A

Combination of multiple peptides or proteins into a single molecule

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18
Q

What is a Monomer?

A

Individual amino acids are monomers of a complete protein structure

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19
Q

What is Hemoglobin made of?

A

4 monomers

20
Q

What is ATP synthase made of?

A

20 monomer (subunits)

21
Q

What does ATP synthase do?

A

Makes ATP molecules inside mitochondria

22
Q

How many amino acids are there in nature?

A

20

23
Q

What is genetic mutation?

A

Change in instructions for making protein.

Lead to amino acid substitutions in making of protein

24
Q

What is denaturation?

A

When environmental conditions can break peptide bonds and bonds within the 3D structure

25
Q

Conditions that cause denaturation?

A

Temperature, pH, ion concentration, enzyme action, physical agitation

26
Q

What does denaturation do to a protein?

A

Causes loss of function

Loss of biological activity

27
Q

What does renaturation do to a protein?

A

Regains activity

28
Q

What is an enzyme?

A

Specialized protein that makes a chemical reaction happen with less activation energy

29
Q

What is activation energy?

A

Energy required to get a reaction started

30
Q

What is another name for enzyme?

A

Catalysts

31
Q

What do anabolic enzymes do?

A

Help to create chemical bonds

Put reactants closer together and in correct orientation

32
Q

What does catabolic enzyme do?

A

Help to break chemical

Pull reactants apart or put them in orientation that stresses the bonds

33
Q

How are enzymes named?

A

The thing they catalyze then -ase

34
Q

What is substrate?

A

The molecules that binds to a particular enzyme

35
Q

What does each enzyme molecule have?

A

An active site

36
Q

What happens at the active site of an enzyme?

A

the reaction takes place

37
Q

What is optimal temperature?

A

Temperature at which they work most efficiently

38
Q

Human enzymes work best at what temperature ?

A

37 degree C

39
Q

What is optimal pH?

A

pH at which enzymes work most efficiently

40
Q

What do inhibitors do?

A

Block the action of an enzyme

41
Q

What are competitive inhibitors?

A

They bind at the active site

42
Q

What is a noncompetitive inhibitors?

A

They bind at another site and changes the shape of the enzyme

43
Q

Another name for noncompetitive inhibitors?

A

Allosteric inhibition

44
Q

When do proteins work best?

A

When they are in their certain environments

Each protein has their own environment

45
Q

What happens when proteins bind to something?

A

They change shape and create a reaction

46
Q

What pH is optimal for human enzymes?

A

7.4

47
Q

What pH is optimal for stomach enzymes?

A

2