Chapter 3 Protein Structure and Folding Flashcards

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1
Q

20 distinct building blocks of proteins (actually 22)

A

amino acids

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2
Q

the central carbon on an amino acids binds to these 4 structures:

A

H - hydrogen atom
NH2 - amino functional group
COOH - carboxyl group
distinctive “R” group, or side chain

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3
Q

in water, amino acids…

A

ionize

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4
Q

in water, the carboxyl group on an amino acid…

A

acts as an acid

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5
Q

in water, the amino group on an amino acid…

A

acts as a base

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6
Q

what makes the 20 amino acids unique from each other? Why?

A

the distinct R group, or side chain

it causes variation in properties

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7
Q

properties of polar and electrically charged R groups:

A

interact readily with water and are hydrophilic, dissolve readily in water

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8
Q

properties of non-polar R groups:

A

lack highly electronegative atoms capable of reacting with water
hydrophobic, coalesce in aqueous solution instead of dissolving

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9
Q

if the R group has a negative charge:

A

it is acidic and will lose a proton

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10
Q

if the R group has a positive charge:

A

it is basic and will pick up a proton

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11
Q

building blocks of polymers

A

monomers

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12
Q

if the R group is uncharged
A. with an oxygen
B. without an oxygen

A

A. the electronegative oxygen will form a covalent bond within the R group, making it an uncharged polar amino acid
B. its a non polar amino acid

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13
Q

meaning of monomer

A

one part

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14
Q

macromolecules

A

large molecules made up of smaller molecule subunits joined together, made up of monomers

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15
Q

monomers linking together:

A

polymerization

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16
Q

amino acids are the ______ that polymerize to form _____

A

monomers, proteins

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17
Q

monomer in, water out, occurs in a ________ reaction

A

condensation

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18
Q

water in, monomer out, occurs in a ________ reaction

A

hydrolysis

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19
Q

monomers polymerize through what type of reaction?

A

condensation reactions/dehydration reactions

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20
Q

polymerization

A

bonding together of monomers

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21
Q

bond between the amino group and the carboxyl group of two acids

A

peptide bond

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22
Q

R group orientation in the peptide backbone:

A

the R groups extend out from the back bone, can react with other R groups and water

23
Q

directionality in the peptide backbone:

A

amino group on one end (N terminus), carboxyl group on one end (C terminus)

24
Q

flexibility in the peptide backbone:

A

the bond on either side of the peptide bond can rotate, so the molecule is flexible

25
Q

polymer with less then 50 amino acids

A

oligopeptide, or peptide

26
Q

oligopeptide

A

few peptides

27
Q

polymer with mire than 50 peptides

A

polypeptides

28
Q

polypeptides

A

many peptides

29
Q

proteins are ____ made up of _________

A

proteins are polymers made up of amino acids

30
Q

Primary structure of proteins is determined by ____ and ______

A

peptide bonds and the unique sequence of amino acids that make up the protein

31
Q

Changes in primary structure affect:

A

protein function

32
Q

Types of bonds that support secondary structure?

A

hydrogen bonds

33
Q

two possible secondary structures:

A

alpha helicies and beta pleated sheets

34
Q

a proteins 3 dimensional shape is determined by its:

A

tertiary structure

35
Q

5 types of bonds that affect tertiary structure

A
  1. hydrogen bonding
  2. hydrophobic interactions
  3. van der waals interactions
  4. covalent bonding (disulfide bonds)
  5. Ionic Bonding (between charged groups)
36
Q

A combination of polypeptide subunits results in:

A

quaternary structure

37
Q

macromolecular machines

A

groups of multiple proteins that assemble to carry out a function

38
Q

dimer

A

protein consisting of 2 identical polypeptide subunits

39
Q

tetramer

A

protein consisting of 2 sets of identical polypeptide subunits

40
Q

how are folding and function related? what happens when a protein is denatured?

A

folding is crucial to function, denaturing a protein breaks disulfide and hydrogen bonds and keeps proteins from working properly

41
Q

which proteins facilitate protein folding?

A

molecular chaperones

42
Q

do proteins only have one shape?

A

no, proteins are somewhat flexible and dynamic, until they are prompted into their functional form

43
Q

Stanley Prusiner on protein folding

A

some proteins are induced to fold into disease causing , infectious agents called prions

44
Q

side effect of prions in several mammals

A

brain degeneration

45
Q

proteins that catalyze are called:

A

enzymes

46
Q

proteins that attack and destry viruses are called:

A

antibodies

47
Q

_____ _______ are responsible for the movement of the cell, and moving large molecules within the cell

A

motor proteins

48
Q

proteins are involved in ________ from cell to cell around the body

A

carrying and receiving signals

49
Q

_______make up body component like skin and nail and form the internal skeleton of cells

A

structural proteins

50
Q

catalyzed reactions involve one or more reactants called :

A

substrates

51
Q

enzymes hold substrates in the exact orientation…

A

to that they can react

52
Q

Emil Fischer’s idea

A

lock and key model of enzymes and substrates

53
Q

where substrates bind to enzymes is the:

A

active site