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Pharmacy BSI > BSI Lecture 3 Protein Function > Flashcards

BSI Lecture 3 Protein Function Flashcards

1
Q

6 Types of Protein Function

A
  1. structural
  2. regulatory
  3. contractile
  4. immunological
  5. transport
  6. catalytic
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2
Q

Structural

A

form structural framework

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3
Q

Regulatory

A

alters cell function (hormones, neurotransmitters, receptors)

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4
Q

Contractile

A

allows shortening of muscle cells

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5
Q

Immunological

A

aid responses that protect body against foreign substances and invading pathogens

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6
Q

Transport

A

carry vital substances throughout body

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7
Q

Catalytic

A

enzymes that regulate biochemical reactions

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8
Q

Proteins interact with what molecule(s) to carry out their functions?

A

ligands

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9
Q

True or False? Ligands have to fit perfectly into their binding site.

A

True

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10
Q

What holds the ligand in place?

A

Many bonds between the ligand and the side chains of the proteins in binding site.

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11
Q

What types of bonds and attractions hold the ligand into the binding site?

A

Non-covalent bonds (hydrogen bonds, ionic bonds, hydrophobic interactions, and Van der Waals attraction)

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12
Q

What determines the function of a protein?

A

Its conformational shape

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13
Q

What determines the types and locations of binding sites

A

shape

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14
Q

True or False? If the conformational shape of a protein changes, the binding site may change.

A

true

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15
Q

What 2 things may happen in regards to the ligand and protein if the conformational shape of the protein changes?

A
  1. ligand will not bind

2. not enough bonds will be made to hold the ligand in place

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16
Q

Define: Denaturation

A

The process in which a protein loses its quaternary, tertiary, and secondary structure present in their native state

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17
Q

What causes protein denaturation?

A

Temperature, pH, Electrolyte concentration

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18
Q

What is disrupted during denaturation?

A

Nonconvalent bonds maintaining secondary, tertiary, and quaternary structure

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19
Q

Define: Protein Turnover

A

Balance between protein building and degrading.

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20
Q

True or False? All proteins have a finite lifetime with in the cell.

A

True

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21
Q

What reasons would cause a protein to degrade?

A

Normal turnover/renewal, mechanism of cellular control, cellular adaptation, damaged, misfolded

22
Q

What is the function of the Ubiquitin-proteasome system?

A

To identify degradation signals on protein to begin the process of degrading a protein

23
Q

What is the first step in the UPS?

A

Protein is tagged with ubiquitin

24
Q

What enzyme recognizes specific degradation signals on proteins and then adds a chain of ubiquitin?

A

Ubiquitin ligases

25
Q

What recognizes tag (chain of ubiquitin) and degrades the protein?

A

Proteasome

26
Q

What are degraded proteins turned back into?

A

peptides

27
Q

What recognizes tag (chain of ubiquitin) and degrades the protein?

A

20s cylinder and 19s caps

28
Q

20s cylinder contains ___________

A

proteases

29
Q

What is the function of the 19s caps?

A

Recognizes ubiquitin on the protein as a tag for destruction and unfolds protein and feeds it into the chamber

30
Q

Enzymes act as a __________, which lowers _________ ________

A

Catalysts; activation energy

31
Q

Define Activation Energy

A

The amount of energy required for a reaction to take place ( to convert the substrate into a transition state)

32
Q

Catalysts convert substrate into product by _______ or _______ _________ bonds.

A

Making; breaking; covalent

33
Q

What do catalyst do?

A

speed up the reaction rate that would normally be slow

34
Q

Coenzyme

A

a small molecule that functions as a transient carrier of a functional group

35
Q

Cofactor

A

inorganic ion or molecule that is required for enzyme activity

36
Q

Why, if a protein denatures, will it lose its function?

A

It causes the protein to lose its shape, the ligand will no longer bind properly to the protein and can no longer perform its function.

37
Q

What type of noncovalent bond assist the ligand to get into position?

A

Hydrophobic interactions.

38
Q

What matters in the function of the protein?

A

Size, shape, and chemical properties

39
Q

Hydrolases

A

hydrolytic cleavage reaction

40
Q

Nucleases

A

break down nucleic acids

41
Q

Proteases

A

break down proteins

42
Q

Synthases

A

synthesize molecules in an anabolic rxn

43
Q

Isomerases

A

rearrange bonds within a single molecule

44
Q

Polymerases

A

polymerization rxn

45
Q

Kinases

A

add phosphate groups to molecules

46
Q

Phosphatases

A

remove phosphate group from molecules

47
Q

Oxido-reductases

A

catalyze rxns in which one molecule is oxidized and the other reduced

48
Q

ATPases

A

hydrolyze ATP

49
Q

Ligases

A

catalyzes condensation rxns in which 2 atoms are joined using ATP or GTP

50
Q

Dehydrogenases

A

remove pairs of hydrogen atoms

Pharmacy BSI (58 decks)

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