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Organic Chemistry Exam #2 > unit 5-7 > Flashcards

unit 5-7 Flashcards

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1
Q

what are the physical properties of lipids?

A
  • soluble in an organic solvent, but insoluble in H2O
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2
Q

what is an acid?

A

a positive ion that donates the proton

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3
Q

what is a base?

A

the base is a proton acceptor (anion charged)

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4
Q

primary proteins

A
  • sequence of amino acids
  • held by peptide bonds
  • no folding/interactions between molecules
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5
Q

secondary proteins

A
  • local folding of peptide chain into helices (a- helix or b-sheet)
  • folding due to hydrogen bonds between the N-H and C=O groups
  • 3D
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6
Q

tertiary proteins

A
  • 3d folding pattern of a protein due to side-chain interactions
  • polar on OUTSIDE
  • non polar on INSIDE
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7
Q

Quarternary proteins

A
  • protein consisting of more than one amino acid chain
    ex. hemoglobin
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8
Q

what are soaps?

A

salts of carboxylic acids

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9
Q

what two parts does soap have?

A

non polar tail and polar head

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10
Q

what are hydrolyzable lipids derived from?

A

fatty acids

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11
Q

what makes up fatty acid?

A

carboxylic acid head and long carbon chain

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12
Q

what do saturated fatty acids have?

A

no double bonds (single bond)

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13
Q

what do unsaturated fatty acids have?

A

they have double bonds and are generally CIS

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14
Q

what are waxes?

A

esters formed from a fatty acid + high molecular weight alcohol

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15
Q

what are triglycerides made up of?

A

three esters formed from glycerol + 3 fatty acids

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16
Q

what does the increase of fatty acid double bonds do to the melting point?

A

decreases the triacylglycerol melting point

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17
Q

what is cholesterol not?

A

water soluble

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18
Q

what two functional groups do amino acids contain?

A

amino & carboxyl group

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19
Q

what is pI?

A

pH at which our molecule has no net charges

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20
Q

what is a zwitterion?

A

when an amino acid contains both a base and acid (+ and - charge on same molecule)

21
Q

what is a basic amino acid?

A

lysine

22
Q

what is an acidic amino acid?

A

asparic acid

23
Q

what is an L- alanine?

A

amine on left of structure

24
Q

what is a D-alanine?

A

amine on right of structure

25
Q

when the pH> isoelectric pH, the ammonium cation __ proton, resulting in the amino acid having a ___ charge

A

lose, negative

26
Q

what is a peptide bond?

A

COO- of amino acid reacts with NH3 of another amino acid

27
Q

dipeptide

A

two amino acids joined by 1 amide bond

28
Q

tripeptide

A

3 amino acids joined by 2 amide bonds

29
Q

London dispersion forces

A

between two nonpolar molecules (WEAKEST)

30
Q

Hydrogen bonding

A

between negative dipole and positive dipole (O-H or N-H) SECOND WEAKEST

31
Q

electrostatic interactions

A

between acidic and basic amino acid side chains (COO- NH3+)

32
Q

disulfide bonds

A

between two sulfur groups (on cysteines) STRONGEST

33
Q

what are fibrous proteins composed of?

A

long linear peptide chain

34
Q

fibrous proteins are ____ in water and serve as ___ roles

A

insoluble, structural

35
Q

what do globular proteins have?

A

polar outside and non polar inside

36
Q

what are globular proteins in water?

A

soluble

37
Q

protein denaturing

A

the process of altering protein shape (NOT breaking peptide bonds)

38
Q

protein hydrolysis

A

driven by enzyme

39
Q

what is an enzyme?

A

proteins that serve as biological catalysts for reactions in all living things

40
Q

what is true about enzymes?

A
  • increase rate of reaction but are unchanged
  • each enzyme catalyzes a certain reaction or type of reaction only
41
Q

what is enzyme activity affected by?

A

both temperature and pH

42
Q

when there is an increase in temperature, what happens to the rate of a chemical reaction?

A

increases as well

43
Q

competitive inhibitor

A

competes with the substrate for binding to the active site

44
Q

noncompetitive inhibitor

A

binds enzyme at a different location than the active site

45
Q

allosteric control

A

binding of regulator to a site on an enzyme that affects its ability to bind a substrate at the active site

46
Q

enzyme inhibitors

A

bind to an enzyme and alter/destroy the enzymes activity to function

47
Q

reversible inhibitor

A

enzyme activity is restored when drug is removed from the environment

48
Q

irreversible inhibitor

A

covalently binds an enzyme, the enzyme is permanently disabled

Organic Chemistry Exam #2 (1 decks)

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