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21 fall: Biochem > lecture 2 > Flashcards

lecture 2 Flashcards

1
Q

prion disease

A

mis-folding of proteins in brain

mad cow

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2
Q

some uses of proteins

A 
enzymatic catalysis
transport
storage
motility
structure and support
immune protection
signaling
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3
Q

four protein structures

A

primary
secondary
tertiary
quaternary

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4
Q

what is basic building blocks of proteins

A

amino acids

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5
Q

general formula for amino acids

A

an alpha carbon attached

  • COOH (carboxyl group)(acidic negative charge)
  • H2N (amino group- + charge)
  • R group (changes per amino acid)
  • H

20 amino acids

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6
Q

molecule with both positive and negative charge

A

zwitterions

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7
Q

are amino acids in L or D formation

A

L

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8
Q

what is primary protein structure

A

just the amino acid sequence

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9
Q

what is secondary protein structure

A

folding/shaping of a local section of polypeptide

a-helix or beta sheet, beta turn. triple helix, coiled coil

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10
Q

what is tertiary protein structure

A

folding of a complete polypeptide chain

Beta sheet and helix of same polypeptide

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11
Q

what is tertiary structure

A

how more than one polypeptide interact with one another

beta sheet/helixes of 2 polypeptides

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12
Q

what is the Vmax of an enzyme reaction?

A

the maximum velocity at which a reaction may occur

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13
Q

what is the Km of an enzyme reaction

A

the amount of substrate needed in order to reach 1/2 of Vmax

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14
Q

at ph 7, every amino acid has a negative charge on its

A

carboxyl group (COO)

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15
Q

polypeptide chains are cross linked by S-S bonds due to

A

cysteine

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16
Q

during chymotrypsin breakdown of a polypeptide, part of the polypeptide is briefly attached covalently to the amino acid

A

serine

17
Q

what effect does an enzyme have on the activation energy of the reaction

A

decreases-

reaction will need less activation energy- reaction is easier to do

18
Q

a competitive enzyme inhibitor will

A

not work well when the substrate concentration is high

19
Q

when an enzyme reaction is inhibited by a noncompetitive inhibitor

A

the Vmax is lowered and Km is unchanged

20
Q

sometimes an enzyme reaction is helped by ATP because ATP transiently transfers its ____ to the substrate

A

phosphate

21
Q

NADH functions as a coenzyme in biological ____ reactions

A

catabolic

22
Q

the enzyme chymotrypsin is secreted from the pancreas as a ____ that needs proteolysis to increase its activity

A

zymogen (chmyotrypsinogen)

23
Q

during the cascade of enzyme reactions that occur in the fight or flight syndrome, majority of the enzyme reactions are stimulated by the attachment of ___ to the enzyme

A

phosphate

24
Q

what is a polar bond

A

non-even share of electrons

usually has + and - side
can be uncharged polar

hydrophilic (like water)
(polar bears like water)

25
Q

non-polar

A

electrons shared evenly- neutral molecule

hydrophobic (hates water)

26
Q

basic has what charge

A

positive charge

27
Q

acid

A

negative charge

28
Q

which amino acid has a SH r group that likes to form disulfide bonds S-S bonds with other animo acids

A

cysteine

29
Q

amino acids form __ bonds and are in ___ chain

A

peptide (covalent)
linear

amino group (NH2)(+) will attach to carboxyl group (COOH)(-)of another animo acid

+ and - parts attach

30
Q

group of amino acids in a chain

A

polypeptide

31
Q

peptide bond

A

water leaves
C of carboxyl group
binds to N of amino group

catalyzed by enzyme

32
Q

breaking of bond by adding water

A

hydrolysis

33
Q

enzyme to break peptide bonds in proteins

A

protease

34
Q

strongest chemical bond when atoms share electrons

A

covalent

35
Q

bonds between opposite charges

A

electrostatic interactions
ionic bonds
salt bridges

36
Q

polar water molecules can form shells around charged surface residue sidechains, helping to stabilize and solubilize the protein

A

water shell and charged surface residues

37
Q

two atoms bearing partial negative charges share a partially positively charged ___ forming a ___ bond

A

hydrogen

hydrogen

38
Q

type of bond when animo acids hate water( non polar)

amino acids will fold onto them selves and hide from water

A

hydrophobic bonds

39
Q

weak electrical attraction of one atom for another, want to be close but not too close

personal space

A

Van der Waal Forces

21 fall: Biochem (44 decks)

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