Lecture 12 Flashcards

1
Q

protein studies

A
  • isolate proteins from samples
  • purify proteins from isolations
  • visualize and size
  • identify
  • use/study
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2
Q

What leads to 2 and 3 degree structures of proteins?

A

R group interactions

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3
Q

Charge of some R groups is….

A

pH dependent

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4
Q

hydrophobic / non polar R groups

A

tend to fold internally

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5
Q

hydrophilic /polar R groups

A

tend to fold externally (to interact with water)

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6
Q

enzyme

A

a protein or RNA that acts as a catalyst for a chemical reaction

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7
Q

Enzymes make reactions…

A

more favourable at physiological conditions

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8
Q

enzyme specificity

A

a product of having the right shape to hold the substrate(s) and a catalytic center to facilitate the reaction

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9
Q

enzyme specificity may require…

A

cofactors like organic molecules (coenzymes) or metal ions

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10
Q

A–>B

A

isomerization

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11
Q

A+B–>C

A

condensation

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12
Q

A–>B+C

A

lysis

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13
Q

A+B–>C+D

A

complicated

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14
Q

reaction rate/velocity

A

v=(-)delta[S]/delta t

v=(+)delta[P]/delta t

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15
Q

Initial Velocity

A

measured quickly and for a short period of time (before 10% of reactants are used up)

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16
Q

rate can be limited by…

A

availability of substrate and by production of product

17
Q

Under optimal conditions and with excess substrate, limiting step is…

A

how fast enzyme can catalyze (ES–>E+P)

18
Q

substrate conc and initial velocity relationship

A

as substrate conc. increases, initial velocity increases

19
Q

Michaelis-Menten Equation

A

Vo=([S]Vmax)/([S]+Km)

20
Q

Km

A

(Michaelis constant) [S] when Vo = 1/2Vmax

21
Q

Km is often neat..

A

the physiological conc. of the substrate in the target cell

22
Q

normal (alcohol)

A

rate from ethanol to acetaldehyde is the same as acetaldehyde to acetic acid

23
Q

allergic (alcohol)

A

acetaldehyde accumulates because rate is different

24
Q

Vmax

A

the enzyme rate as we increase [S]

25
Q

turnover number

A

-kcat=vmax/[E]T

26
Q

Lineweaver-Burk

A

uses double reciprocal of rate and conc. to place Vmax and Km on X and Y intercepts

27
Q

Km values can be used to..

A

investigate affinity of an enzyme for a substrate and compare reaction rates in more complicated living systems

28
Q

competitive inhibition

A

a compound binds to active site of enzyme and excludes reactant
-lower affinity of enzyme

29
Q

uncompetitive inhibition

A

[up=up] a compound binds the ES complex and slows transition to EP

30
Q

non-competitive inhibition

A

a compound binds the enzyme and change shape of active site