exam one cram notecards Flashcards

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1
Q

isolectric point and anion exchange

A

Pi>pH:protein is positively charged and will bind to cation exchange
pH>Pi: Protein is negativelt charged will bind to anion exchange

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2
Q

Ramachandran

A

Axis: X:psi, Y:phi
Gly: no restriction
Pro: restriction

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3
Q

Competitive inhibition

A

Binds to enzyme, changes slope and Km but not y int
multiply Km by alpha

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4
Q

uncompetitive inhibiton

A

binds to ES, same slope dif Y int and Km. a’/Vmax

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5
Q

noncompettivie

A

Both things,

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6
Q

a helix numbers

A

1.5 Angstroms/residue
3.6 residues per term

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7
Q

Cholera toxin symmetry

A

C5 symmetry

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8
Q

GroEL symmetry

A

C7

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9
Q

Where does trypsin cut? chemotrypsin?

A

Trypsin: Lys, Arg
Chemotryp: Try, trp, phe, leu
BOTH BLOCKED BY PROLINE

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10
Q

hemoglobin symmetry

A

C2

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11
Q

HIll coefficient

A

If hill>1=cooperative
if hill<1=not cooperative

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12
Q

bohr effect on hb

A

ph decrease, histidine protonated, salt bridge stronger, decrease O2 binding, more o2 to muscles. Shifts sigmoidal curve left

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13
Q

BPG

A

Shifts curve right
decreases HB affinity for O2, increases 02 delivery to tissue

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14
Q

RNase A mechanism

A

histidines carry out the acid base catalysis
1. his acts as base, takes H+ from 2 OH
2. O-nucleophillic attack
3. histidind 2 acts as acid, gives H+
4. 2,3 cyclic intermediate formed

Then
1. histidine2 acts as base, takes H+ from H2O
2. water OH is nucleophile, attakcs phosphate intermediate
3. his 1 acts as acid, gives H+
4. 2nd product formed

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15
Q

metal ion catalysis

A

Zinc coordinated by three histidines
zn polarizes H2O which ionizes bc the 4th histidine
OH nucleophillic attack on C of CO2
bicarbonate formed

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16
Q

covalent catalysis

A

cov bond is temporarily formed between enzyme and substrate

17
Q

Trypsin

A

-All B protein
similar to chymotrpysin and elastase, same cat triad but diff specificity

18
Q

Catalytic triad

A

Aspartate: orients histadine
histadine:under goes acid base catalysis
serine: does covalent catalysis

19
Q

Features of serine protease mechanism

A

covalent catalysis to create a covalent intermediate (tetrahedral)
concerted acid base catalysis
transition state stabilization via the oxyanion hole
covalent bond formation that transiently turns trigonal C to tetrahedral intermediate
tetrahedral oxyanion intermediate that stabilizes the transition state

20
Q

ATCase

A

12 subunits, D3 symmetry
feeback inhibited by CTP
ATP stimulates ATCase
CTP binds T state(less active)
ATP binds R state(more active)
PALA shifts T->R

21
Q

no polar pneumonic

A

GAVLIMP

22
Q

polar pneumonic

A

STAGC

23
Q

+ charge

A

HAL