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Flashcards in Proteins Deck (75):
1

the functional groups

amine group and carboxyl group

2

how many amino acids in a protein

20

3

what is L vs D

L/levo: amine group on the left;
D/dextro: amine group on the right

4

what is a peptide bond; what type

amine group to carboxyl; covalent

5

what is the first amino acid of all proteins

aug

6

monomers of proteins

amino acid

7

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

hydrolysis

8

2 amino acid

dipeptide

9

oligopeptide

3-10 amino acids

10

more than 10 amino acid

polypeptide

11

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

polypeptide; 350

12

how many essential AA

10

13

how many nonessential AA

10

14

how do we get essential AA

must be eaten

15

how do we get nonessential AA

we make them

16

how many proteins in a cell and how long they last

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

17

what are the 4 types of R groups

basic, acidic, polar, nonpolar

18

name the basic R groups

lysine, arginine, histidine

19

what makes an R group basic

positive charge

20

how to help recognize a basic R group

NH

21

name the acidic R groups

aspartic acid, glutamic acid

22

what makes an R group acidic

neg charge (donate protons)

23

how to recognize an acidic r group

C double bonded to O and bonded to O

24

how to recognize an uncharged polar R group

OH

25

charge of polar R groups

neutral

26

how to help recognize a nonpolar R group

CH

27

charge of nonpolar R group

neutral

28

what allows for the "mirror image" isomers

the alpha carbon is asymmetric

29

types of protein functions: enzyme

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

30

types of protein functions: structural protein

holds up (provides mechanical support)

31

types of protein functions: transport protein

carries small molecules or carbons;
example: hemoglobin carries oxygen

32

types of protein functions: motor protein

slide filaments (generates movement)

33

types of protein functions: storage protein

stores small molecules

34

signal protein

tells cells to ______ (carries signals between cells)

35

types of protein functions: receptor proteins

detects signals (and transmits them)

36

types of protein functions: gene regulatory protein

switch genes on/off (p53)

37

types of protein functions: special purpose proteins

varied

38

how many AA commonly found in proteins

20

39

what process do AA bond

dehydration synthesis

40

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

R groups; charge

41

what form are most proteins in

globular (folded)

42

what decided the shape of a protein

AA sequence

43

what are the four noncovalent forces found in protein folding

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

44

ionic bonding

positive to negative

45

hydrogen bonding

positive hydrogen to negative oxygen

46

VanDer Wahls forces

atoms forced close to each other (weak)

47

hydrophobic interactions

they turn in to avoid water

48

what is the primary level of protein structure

amino acid sequence (always!)

49

what is the secondary level of protein structure

common folding patterns

50

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

1. alpha helix- "slinky"
2. beta sheet- "elongated slinky"

51

what is the tertiary level of protein structure

3-D shape (final)

52

what is the quarternary level of protein structure

more than 1 polypeptide (1 protein, multiple polypeptides)

53

conformation

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

54

native protein

normal, natural state

55

denatured

lost its shape

56

what are the 2 factors that can denature a protein

temperature, pH-isoelectric point

57

why does temp denature

hotter, breaks weak bonds, changes shape

58

isoelectric point

pH at which a protein becomes neutral

59

negative has _____ isoelectric points

low

60

positive have _____ isoelectric points

high

61

components of enzymes

-most* are proteins (*rna)
-shape is important
-specific
-not changed, used repeatedly

62

enzyme equation

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

63

what are E, S, and P

Enzyme, substrate, product

64

what happens to the substrate

it is altered permanently (into the product)

65

what enzyme would digest a fat

lipase

66

at high temps the rate of enzyme action decreases because

the increased heat alters the site of the active enzyme

67

enzymes influence chemical reactions in living systems by

affecting the rate at which reactions occur

68

which group of organic compounds includes enzymes

proteins

69

what does the lock and key hypothesis attempt to explain

mechanism of enzyme specificity

70

a substance acted upon by an enzyme

substrate

71

enzymes are

specific

72

at 0°C most enzymes are

inactive

73

what enzyme is in maltase but not maltose

nitrogen

74

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

light present

75

lipase, maltase, and protease are examples of

enzymes