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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
Enzymatic factors that affect rates (4)
- 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
26
Holoenzyme
apoenzyme and a prosthetic group
27
apoenzymes
enzymes that need prosthetic groups in order to be functional
28
cofactors
inorganic | usually metal ions (Mg, Fe, Zn) that are required by certain enzymes
29
example of a cofactor
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
coenzymes
organic | vitamins and carrier molecules
31
example of a coenzyme
pyruvate dehydrogenase: - requires thiamine (B1) to act as electron sink for carboxylation of pyruvate - alcoholics have issues with B1
32
Enzymes : Inhibitors
either prevent the binding of E to S or prevent the E from converting S to P
33
Competitive inhibitors
resemble S and bind to active site
34
Noncompetitive inhibitors
bind to allosteric site and alter the shape of or access to the active site
35
Inhibition can be...
reversible or irreversible
36
substrate level inhibition
occurs when an enzyme has 2 binding sites for the substrate (active and allosteric)
37
active site vs allosteric site
have diff Km and have diff affinities, bind at diff concentrations
38
binding at the allosteric site_____ at the active site
decreases the binding/conversion
39
What is substrate level inhibition useful for?
metabolic regulation and toxin mitigation
40
lower Km what affinity binds to it
higher affinity
41
higher km what affinity binds to it
low affinity
42
When you have a little bit of substrate...
it will go to the higher affinity, lower Km
43
When you have lots of substrate...
it will bind to the lower affinities since there is more of it and a higher Km
44
Application of substrate level inhibition: Phosphofructose Kinase
- 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
What happens if you run out of ATP (substrate level inhibition)
the allosteric site does not pick it up and the rxn goes forward - there is not enough to bind to the inhibitor site
46
What molecule level is being stabilized in substrate level inhibition of phosphofructose kinase?
ATP | - when more than enough ATP process slows to not waste energy
47
Application: Substrate Level Inhibition: Toxin Mitigation | What catalyzes the first step in the detoxification of alcohol?
alcohol dehydrogenase
48
acetate
nontoxic
49
alcohol
strong substrate level inhibition
50
acetaldehyde
highly toxic, vomiting, damage liver and heart, CNS
51
What happens when you get a build of acetaldehyde ?
you get nauseous quickly after drinking, skin flushes, enzymes not working well (Sami)
52
What happens when the conversion to the intermediate is slowed down?
most negative effects can be somewhat mitigated
53
increase in alcohol, it binds to the _____.....
allosteric site slowing it down to mitigate dangerous effects of intermediate , minimizes toxicity
54
product level inhibition
product binds to an allosteric site on the enzyme to slow the reaction - involved in metabolic regulation
55
Example of product level inhibition
hexokinase and Kreb's cycle enzymes | inhibition ensures glucose will not be dedicated to ATP production unless the cell is utilizing it
56
Km
affinity of E for S lower the Km, higher the affinity [S] at 1/2 Vmax
57
Vmax
capacity of E to handle fluctuations in S | when all E is in the ES complex
58
isoenzymes
catalyze the same reaction but have different activity levels due to minor structural changes
59
Isoenzymes are ____ specific
tissue specific
60
hexokinase vs glucokinase
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
Application isoenzymes: what can G-6-P be directed to
glycolysis and cellular respiration
62
under conditions of high ATP and low ADP, Kreb's cycle enzymes will ______
not move the process forward
63
Build up of citrate will stimulate...
biosynthesis of fatty acids
64
What would happen to the liver in a consistently high sugar environment?
- 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
What does an increase in an isoenzyme in the bloodstream indicate?
you have had tissue damage | - dying cells released into bloodstream
66
CPK1
brain, lungs
67
CPK2
heart
68
CPK3
skeletal muscle

Anatomy and Physiology I (17 decks)

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