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Anatomy and Physiology I > Exam 2: Macromolecules: Proteins > Flashcards

Exam 2: Macromolecules: Proteins Flashcards

1
Q

Functions of proteins (8)

A
  • structure, hormones/signaling, neurotransmitters, blood clotting, viscosity, antibodies, transport, enzymes
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2
Q

What is the monomer of a protein and what is the chiral isomer?

A

amino acid

L-form

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3
Q

What does a monomer of a protein consist of

A

amino group, carboxyl group, R group (variation)

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4
Q

What type of rxns form peptide bonds?

A

dehydration rxns

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5
Q

Characteristics of peptide bonds (3)

A
  • trans configuration
  • planar
  • rotation at bond
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6
Q

4 levels of protein structure

A

primary, secondary, tertiary, quaternary

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7
Q

Primary protein structure

A

amino acid sequence stabilized by peptide bonds

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8
Q

Secondary protein structure

A

alpha helix, beta pleated sheets

stabilized by interactions with primary carbonyl and amine groups forming domains

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9
Q

Tertiary protein structure

A

interaction between R groups
- covalent bonding, ionic interaction, hydrophobic interaction, hydrogen bonding
3D shape

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10
Q

Quaternary protein structure

A

interactions between peptide chains

same bonding types as tertiary

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11
Q

Chaperone proteins

A

first identified as heat shock proteins
- provide favorable environment for correct folding, prevents unfolding or unfolded proteins from forming aggregates, being degraded, or folding into toxic molecules

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12
Q

What diseases exhibit abnormal folding?

A

prion diseases

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13
Q

What are prions and what are some diseases they cause?

A

infectious proteins

cause: bovine spongiform encephalopathy, Creutzfeldt-Jakob, kuru, fatal familial insomnia

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14
Q

Where do prion proteins most commonly occur?

A

brain

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15
Q

What role do normal cellular PrPc prions have?

A

protective role

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16
Q

What PrPsc (scrapes)

A

abnormally folded proteins that form insoluble aggregates

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17
Q

What is the problem with protein aggregates?

A

they damage neurons and are resistant to degradation

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18
Q

PrPsc induce PrPc prions to convert…

A

increasing the number of dangerous prions

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19
Q

How did cows get mad cow (bovine)?

A

from calcium supplements (from bones of sheep) , sterilization can not kill off prions

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20
Q

Tissue Damage from prion diseases

A

holes in the brain, damaged brain tissue
motor function effected
prevents cell from functioning

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21
Q

What 2 diseases has research about prion diseases shed light on?

A

Alzheimer’s disease and Huntington’s Chorea

  • all of these diseases involve neurotoxicity
  • all have amyloid plaque formation
  • misfolding exposes hydrophobic groups
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22
Q

Enzymes

A
  • protein based
  • highly specific for substrate
  • catalyze all metabolic reactions by lowering the Ea
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23
Q

What type of reaction do you get when you have a negative change in free energy?

A

spontaneous reaction

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24
Q

How would a positive change in free energy make a rxn go forward?

A

if it was linked to a strongly negative reaction (hydrolysis of ATP)

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25
Q

Enzymatic factors that affect rates (4)

A
  • with unlimited substrate, the enzyme concentration willl continue to rise
  • reaction continues until all the enzyme is in the enzyme substrate complex, Vmax
  • pH : affects charge and reactivity of active site
  • T: rate increases until denaturation occurs
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26
Q

Holoenzyme

A

apoenzyme and a prosthetic group

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27
Q

apoenzymes

A

enzymes that need prosthetic groups in order to be functional

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28
Q

cofactors

A

inorganic

usually metal ions (Mg, Fe, Zn) that are required by certain enzymes

29
Q

example of a cofactor

A

ATPases:

- require Mg2+ cofactor to put stress on the high energy bonds, it weakens the bond so it can be broken to get energy

30
Q

coenzymes

A

organic

vitamins and carrier molecules

31
Q

example of a coenzyme

A

pyruvate dehydrogenase:

  • requires thiamine (B1) to act as electron sink for carboxylation of pyruvate
  • alcoholics have issues with B1
32
Q

Enzymes : Inhibitors

A

either prevent the binding of E to S or prevent the E from converting S to P

33
Q

Competitive inhibitors

A

resemble S and bind to active site

34
Q

Noncompetitive inhibitors

A

bind to allosteric site and alter the shape of or access to the active site

35
Q

Inhibition can be…

A

reversible or irreversible

36
Q

substrate level inhibition

A

occurs when an enzyme has 2 binding sites for the substrate (active and allosteric)

37
Q

active site vs allosteric site

A

have diff Km and have diff affinities, bind at diff concentrations

38
Q

binding at the allosteric site_____ at the active site

A

decreases the binding/conversion

39
Q

What is substrate level inhibition useful for?

A

metabolic regulation and toxin mitigation

40
Q

lower Km what affinity binds to it

A

higher affinity

41
Q

higher km what affinity binds to it

A

low affinity

42
Q

When you have a little bit of substrate…

A

it will go to the higher affinity, lower Km

43
Q

When you have lots of substrate…

A

it will bind to the lower affinities since there is more of it and a higher Km

44
Q

Application of substrate level inhibition: Phosphofructose Kinase

A
  • if ATP increases, it will bind to the active site and the allosteric site making it harder to move forward
    • do not put energy into it until there is a dec in ATP
45
Q

What happens if you run out of ATP (substrate level inhibition)

A

the allosteric site does not pick it up and the rxn goes forward
- there is not enough to bind to the inhibitor site

46
Q

What molecule level is being stabilized in substrate level inhibition of phosphofructose kinase?

A

ATP

- when more than enough ATP process slows to not waste energy

47
Q

Application: Substrate Level Inhibition: Toxin Mitigation

What catalyzes the first step in the detoxification of alcohol?

A

alcohol dehydrogenase

48
Q

acetate

A

nontoxic

49
Q

alcohol

A

strong substrate level inhibition

50
Q

acetaldehyde

A

highly toxic, vomiting, damage liver and heart, CNS

51
Q

What happens when you get a build of acetaldehyde ?

A

you get nauseous quickly after drinking, skin flushes, enzymes not working well (Sami)

52
Q

What happens when the conversion to the intermediate is slowed down?

A

most negative effects can be somewhat mitigated

53
Q

increase in alcohol, it binds to the _____…..

A

allosteric site slowing it down to mitigate dangerous effects of intermediate , minimizes toxicity

54
Q

product level inhibition

A

product binds to an allosteric site on the enzyme to slow the reaction
- involved in metabolic regulation

55
Q

Example of product level inhibition

A

hexokinase and Kreb’s cycle enzymes

inhibition ensures glucose will not be dedicated to ATP production unless the cell is utilizing it

56
Q

Km

A

affinity of E for S
lower the Km, higher the affinity
[S] at 1/2 Vmax

57
Q

Vmax

A

capacity of E to handle fluctuations in S

when all E is in the ES complex

58
Q

isoenzymes

A

catalyze the same reaction but have different activity levels due to minor structural changes

59
Q

Isoenzymes are ____ specific

A

tissue specific

60
Q

hexokinase vs glucokinase

A

glucokinase is a type of hexokinase

hexokinase: found in most tissues (brain, muscle) and is the “maintenance” enzyme - hard to upregulate
glucokinase: found primarily in the liver upregulated more than hexokinase

61
Q

Application isoenzymes: what can G-6-P be directed to

A

glycolysis and cellular respiration

62
Q

under conditions of high ATP and low ADP, Kreb’s cycle enzymes will ______

A

not move the process forward

63
Q

Build up of citrate will stimulate…

A

biosynthesis of fatty acids

64
Q

What would happen to the liver in a consistently high sugar environment?

A
  • build up of fat in liver
  • liver can make G6P, no inhibition , pushing glycolysis get to Krebs, it says no and you can make fat and glycogen
    liver trying to process extra sugar
65
Q

What does an increase in an isoenzyme in the bloodstream indicate?

A

you have had tissue damage

- dying cells released into bloodstream

66
Q

CPK1

A

brain, lungs

67
Q

CPK2

A

heart

68
Q

CPK3

A

skeletal muscle

Anatomy and Physiology I (17 decks)

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