Midterm 1 Flashcards

1
Q

Alpha Helix

A

Parallel

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2
Q

Alpha Helix problems that can occur

A

Electrostatic Repulsion (i.e. 2 basic AA)
Crowding - 2 Bulky R Group
Bend - Proline

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3
Q

Beta Sheets

A

Perpendicular

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4
Q

Reverse Turn

A

3 Residues, Proline, Glycine

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5
Q

Trpsin

A

Arginine and Lysine, C-terminus

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6
Q

Chymotrypsin

A

Trp, Phe, Tyr (ring structures)

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7
Q

CNBr

A

Met

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8
Q

Km

A

Binding Affinity, how much substrate is needed to reach 1/2Vmax

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9
Q

Smaller the Km,

A

Greater the Binding affinity

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10
Q

Vmax

A

Max Rate, depends on enzyme itself

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11
Q

Turnover Rate

A

How much it turns substrate into product per amount of enzyme
kcat=Vmax/[Total Enzyme]

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12
Q

Michaels Menten

A

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

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13
Q

Lineweaver Burk

A

1/V=Km/Vmax (1/[S]) + 1/Vmax

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14
Q

x-intercept=

A

xintercept=1/KM

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15
Q

Slope=

A

Slope=Km/Vmax

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16
Q

y-intercept=

A

1/Vmax

17
Q

Competitive Inhibition

A

Km (binding affinity) increase

more substrate will be needed to bind to the enzyme

18
Q

Noncompetitive Inhibition

A

Vmax decrease

19
Q

Uncompetitive Inhibition

A

Binding when E and S come together
Affects K and Vmax
Parallel lines

20
Q

Mixed Inhibition

A

Binding of S can affect inhibitor, vice versa

Will cross in the left quadrant

21
Q

R-state

A

Active, high binding affinity for substrate

Activators causes R-state

22
Q

T-state

A

Inactive, low binding affinity for substrate

Inhibitors cause T-state

23
Q

Sequential model for binding of substrate

A

T to R, causes next one to turn T to R

24
Q

Phosphorylation

A

can turn off or on the protein

Modifies the actual enzyme, on hydroxy group amino acids (Serine, Theronine, Tyrosine)

25
Q

Coenzyme

A

Participates in enzymes, not proteins. NAD, NAD+

26
Q

Why is Induced fit more probable?

A

Transition State
Lower Activation energy
If E and S bind too perfectly, the diff. between ES and EX(transition) would be too large to overcome

27
Q

Non-allosteric enzyme curve

A

1st order, then 0 order as [S] increased