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Biology > Proteins > Flashcards

Proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

the functional groups

A

amine group and carboxyl group

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2
Q

how many amino acids in a protein

A

20

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3
Q

what is L vs D

A

L/levo: amine group on the left;

D/dextro: amine group on the right

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4
Q

what is a peptide bond; what type

A

amine group to carboxyl; covalent

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5
Q

what is the first amino acid of all proteins

A

aug

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6
Q

monomers of proteins

A

amino acid

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7
Q

when you digest proteins what process breaks them down into amino acids

A

hydrolysis

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8
Q

2 amino acid

A

dipeptide

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9
Q

oligopeptide

A

3-10 amino acids

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10
Q

more than 10 amino acid

A

polypeptide

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11
Q

the type of most proteins (# of amino acids) and how many they typically have

A

polypeptide; 350

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12
Q

how many essential AA

A

10

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13
Q

how many nonessential AA

A

10

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14
Q

how do we get essential AA

A

must be eaten

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15
Q

how do we get nonessential AA

A

we make them

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16
Q

how many proteins in a cell and how long they last

A

1 billion; about a week (we are constantly making them)

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17
Q

what are the 4 types of R groups

A

basic, acidic, polar, nonpolar

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18
Q

name the basic R groups

A

lysine, arginine, histidine

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19
Q

what makes an R group basic

A

positive charge

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20
Q

how to help recognize a basic R group

A

NH

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21
Q

name the acidic R groups

A

aspartic acid, glutamic acid

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22
Q

what makes an R group acidic

A

neg charge (donate protons)

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23
Q

how to recognize an acidic r group

A

C double bonded to O and bonded to O

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24
Q

how to recognize an uncharged polar R group

A

OH

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25
Q

charge of polar R groups

A

neutral

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26
Q

how to help recognize a nonpolar R group

A

CH

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27
Q

charge of nonpolar R group

A

neutral

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28
Q

what allows for the “mirror image” isomers

A

the alpha carbon is asymmetric

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29
Q

types of protein functions: enzyme

A

speeds up chemical reaction (by catalyzing covalent bond breakage or formation)

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30
Q

types of protein functions: structural protein

A

holds up (provides mechanical support)

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31
Q

types of protein functions: transport protein

A

carries small molecules or carbons;

example: hemoglobin carries oxygen

32
Q

types of protein functions: motor protein

A

slide filaments (generates movement)

33
Q

types of protein functions: storage protein

A

stores small molecules

34
Q

signal protein

A

tells cells to ______ (carries signals between cells)

35
Q

types of protein functions: receptor proteins

A

detects signals (and transmits them)

36
Q

types of protein functions: gene regulatory protein

A

switch genes on/off (p53)

37
Q

types of protein functions: special purpose proteins

A

varied

38
Q

how many AA commonly found in proteins

A

20

39
Q

what process do AA bond

A

dehydration synthesis

40
Q

what causes proteins to fold; and what is it based on

A

R groups; charge

41
Q

what form are most proteins in

A

globular (folded)

42
Q

what decided the shape of a protein

A

AA sequence

43
Q

what are the four noncovalent forces found in protein folding

A

ionic bonding, hydrogen bonding, VanDer Wahls forces, hydrophobic interactions

44
Q

ionic bonding

A

positive to negative

45
Q

hydrogen bonding

A

positive hydrogen to negative oxygen

46
Q

VanDer Wahls forces

A

atoms forced close to each other (weak)

47
Q

hydrophobic interactions

A

they turn in to avoid water

48
Q

what is the primary level of protein structure

A

amino acid sequence (always!)

49
Q

what is the secondary level of protein structure

A

common folding patterns

50
Q

what are the common folding patterns in the secondary level or protein structure

A
  1. alpha helix- “slinky”

2. beta sheet- “elongated slinky”

51
Q

what is the tertiary level of protein structure

A

3-D shape (final)

52
Q

what is the quarternary level of protein structure

A

more than 1 polypeptide (1 protein, multiple polypeptides)

53
Q

conformation

A

overall, final 3-D shape (use x-ray diffraction)

54
Q

native protein

A

normal, natural state

55
Q

denatured

A

lost its shape

56
Q

what are the 2 factors that can denature a protein

A

temperature, pH-isoelectric point

57
Q

why does temp denature

A

hotter, breaks weak bonds, changes shape

58
Q

isoelectric point

A

pH at which a protein becomes neutral

59
Q

negative has _____ isoelectric points

A

low

60
Q

positive have _____ isoelectric points

A

high

61
Q

components of enzymes

A
  • most* are proteins (*rna)
  • shape is important
  • specific
  • not changed, used repeatedly
62
Q

enzyme equation

A

E+S–>ES(noncovalent bond here)–>EP–>E+P

63
Q

what are E, S, and P

A

Enzyme, substrate, product

64
Q

what happens to the substrate

A

it is altered permanently (into the product)

65
Q

what enzyme would digest a fat

A

lipase

66
Q

at high temps the rate of enzyme action decreases because

A

the increased heat alters the site of the active enzyme

67
Q

enzymes influence chemical reactions in living systems by

A

affecting the rate at which reactions occur

68
Q

which group of organic compounds includes enzymes

A

proteins

69
Q

what does the lock and key hypothesis attempt to explain

A

mechanism of enzyme specificity

70
Q

a substance acted upon by an enzyme

A

substrate

71
Q

enzymes are

A

specific

72
Q

at 0°C most enzymes are

A

inactive

73
Q

what enzyme is in maltase but not maltose

A

nitrogen

74
Q

what is an environmental condition that has the LEAST effect on the rate of enzyme controlled reactions

A

light present

75
Q

lipase, maltase, and protease are examples of

A

enzymes

Biology (19 decks)

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