Biochemistry 1 Flashcards

1
Q

catalysts

A
  • increase the rate of the reaction by
    • stabilizing the TS
    • reduce Ea
    • does not change ΔG. cannot make a nonspontaneous reaction spontaneous.
    • kinetic not thermodynamic role.
    • take an already spontaneous reaction and make it go faster.
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2
Q

3 defining characteristics of enzymes/catalysts

A
  • must increase reaction rate
  • must not be used up in the reaction - regenerated
  • specific for a particular reaction
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3
Q

lock and key model

A
  • substrate and active site are perfectly complementary
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4
Q

induced fit model

A
  • binding of substrate causes conformational change in enzyme.
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5
Q

active site of an enzyme stereospecificity

A
  • L amino acids (LA)

- D sugars/carbs (DC)

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6
Q

Vmax depends on

A
  • enzyme concentration

- type of enzyme you have

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7
Q

Km

A
  • the concentration of substrate required to reach 1/2 Vmax

- higher affinity has smaller Km

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8
Q

competitive inhibition

A
  • binds reversibly at active site
  • no change on Vmax
  • increases Km
  • overcome by adding more substrate
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9
Q

non-competitive inhibition

A
  • binds at allosteric site
  • reduces Vmax
  • no change on Km
  • adding more substrate does not help.
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10
Q

uncompetitive inhibition

A
  • binds at allosteric site of ES complex
  • reduces Vmax
  • reduces Km
  • limits amount of ES to be converted to product
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11
Q

mixed inhibition

A
  • binds at allosteric site of E alone or ES complex
  • reduces Vmax
  • Km varies
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12
Q

if inhibitor has affinity for ES complex

A
  • looks more like uncompetitive
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13
Q

if inhibitor has affinity for enzyme

A
  • looks like competitive
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14
Q

if inhibitor has equal affinity for enzyme and ES complex

A
  • looks like non competitive.
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15
Q

4 biologically relevant macromolecules

A
  • proteins
  • carbohydrates
  • lipids
  • nucleic acids
  • all polymers
  • enzymes that make them are called polymerases
  • run in polymerization reactions or dehydration synthesis
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16
Q

pH < pka

A

will be positively charged

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17
Q

ph > pka

A

will be negatively charged

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18
Q

ph = pka

A

will be neutral (zwitterion)

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19
Q

acidic amino acid has

A

(-) charge at physiological pH

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20
Q

basic amino acid has

A

(+) charge at physiological pH

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21
Q

2 covalent bonds in proteins

A
  • peptide bond

- disulfide bridge between cysteines.

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22
Q

primary structure of protein

A
  • amino acid sequence

- determined by peptide bond

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23
Q

secondary structure of protein

A
  • hydrogen bonding interactions between backbone atoms
  • alpha helix
  • beta pleated sheet
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24
Q

why is proline not found in the alpha helix

A
  • will cause kink
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25
same direction beta sheet
- parallel
26
opposite direction beta sheet
- antiparallel
27
denatured protein
- improperly folded
28
denaturation
- disruption of protein structure without breaking peptide bonds - urea - extreme pH and temp - change in salt concentration (tonicity)
29
tertiary structure
- due to side chain interactions within a peptide | - noncovalent and covalent
30
noncovalent interactions in tertiary structure
- polar/polar - nonpolar/nonpolar - acidic/basic - electrostatic
31
covalent interactions in tertiary structure
- disulfide bridge - found in extracellular protein - stabilizes tertiary protein structure.
32
quaternary structure
- structure due to side chain interactions between different polypeptide subunits - no peptide bonds found
33
monomer of carbs
- monosaccharide | - CnH2nOn
34
3 common sugars
- glucose - 6 membered - fructose - 5 membered - galactose C6H12O6
35
3 common disaccharides
- maltose (glucose + glucose) alpha 1-4 - sucrose (glucose + fructose) alpha 1-2 - lactose (glucose + galactose) beta 1-4
36
formula for disaccharides
C12H22O11 C12H24O12 - H2O
37
multiple monosaccharides
- polysaccharides
38
3 common polysaccharides
- glycogen - animal storage (alpha 1-4 for residues, 1-6 for linking) - starch - plant storage (alpha) - cellulose - plant structure (beta 1-4, 1-6)
39
functions of polysaccharides
- energy - cell surface markers - cell adhesion
40
hydrocarbon
- monomer of lipid - long unsubstituted alkane that ends in a carboxylic acid - synthesized 2 carbons at a time
41
saturated fatty acid
- covalently bound to maximum number of hydrogen - solid at room temperature (worse for body) - no double bonds - more rigid less fluid
42
unsaturated fatty acid
- one or more double bonds - Z or cis - liquid at room temperature (better for body) - disrupts packing
43
amphoteric
- acts as acid or base
44
amphiphilic
- both polar and nonpolar
45
triglyceride
- stored energy - glycerol - 3 fatty acids
46
why are fats more more efficient for energy storage than carbs
- packing - hydrophobicity allows great, close packing | - energy content - more energy carbon for carbon. more reduced so when they are oxidized produce more energy.
47
phospholipids
- barrier between intracellular and extracellular environments - form lipid bilayer - driven by hydrophobic interactions. stabilized by van der waals forces between tails
48
what determines fluidity
- saturation - tail length - amount of cholesterol
49
how many isoprenes to make a terpene?
- 3 | - must have 2 isoprenes minimal to make a terpene
50
function of terpenes
- precursor to cholesterol, ear wax | - vitamin A terpenoid
51
cholesterol
- 666 + 5 - obtained from diet - synthesized in liver - carried in blood w/ fats and proteins (lipoproteins)
52
functions of cholesterol
- cell membranes - precursors to steroids - bile
53
cholesterol at low temps cholesterol at high temps
- increases fluidity - decreases fluidity - paradox
54
solving for enthalpy
ΔH = E + PΔV
55
reduced form of the disulfide bond
- broken | - cysteine's acquiring H's
56
exergonic
- (-)ΔG | - products lower in energy than reactants
57
endergonic
- (+)ΔG | - reactants lower in energy than products
58
squalene is how many isoprenes
- 6 | - 3 terpenes
59
ATP hydrolysis
- 30.5 kJ | - 12 kcal/mol
60
how fast something will happen?
- kinetics
61
cofactor
- metal ions or small molecules
62
coenzyme
- cofactor that is an organic molecule
63
to switch an enzyme to on/off
- phosphorylation | - allosteric regulation
64
allosteric regulation
- bind somewhere other than active site (allosteric site) to modify enzyme function.
65
positive feedback regulator
- must have external regulator.
66
y intercept in LB
1/vmax
67
x intercept in LB
-1/Km