Chapter 16

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1

classify protein according to its function:
hemoglobin, oxygen carrier in the blood

transport

2

classify protein according to its function:
collagen, a major component of tendons and cartilage

structural

3

classify protein according to its function:
keratin, a protein found in hair

structural

4

classify protein according to its function:
amylases that hydrolyze starch

enzyme

5

classify protein according to its function:
insulin, a protein needed for glucose utilization

hormone

6

classify protein according to its function:
antibodies, proteins that disable foreign proteins

protection

7

classify protein according to its function:
casein, milk protein

storage

8

classify protein according to its function:
lipases that hydrolyze lipids

enzyme

9

what functional groups are found in all alpha amino acids

carboxylic acid an amino group

10

protein that consists of long, thin, fiber like shapes.

fibrous

11

proteins that make up structural tissues such as hair, wool, skin and nails

fibrous

12

proteins that have spherical shapes

globular

13

proteins that carry out the functions of the cells such as synthesis, transport and metabolism

globular

14

found in eggs, milk, meat, fish an poultry

essential amino acids

15

R is hydrocarbon or aromatic

nonpolar

16

hydrophobic

nonpolar

17

R contains polar molecule such as OH

polar

18

hydrophilic

polar

19

R contains COOH group

acidic

20

R contains NH2 group

basic

21

during ionization of amino acid the COOH group donates or accepts a proton?

donates

22

during ionization of amino acid the NH2 donates or accepts a proton

accepts

23

In solutions near neutral pH, most amino acids exist in the ionized form called the

Zwitterion

24

the Zwitterion has a net charge of

zero

25

in basic solutions the NH3 donates a proton thus forming an ion with a positive or negative charge?

negative

26

in acidic solutions the COO- accepts a proton thus forming a ion with a positive or negative charge

positive

27

in acidic solutions the COO- accepts or donates a proton

accepts

28

in acidic solutions the NH3 accepts or donates a proton

donates

29

peptide bonds can be broken by

hydrolysis

30

secondary structure is determined by

the amino acid sequence, the primary structure

31

folding of the primary structure into a specific shape

secondary structure

32

held together by H bonds between N-H and C=O

secondary structure

33

three main secondary structures shapes

alpha helix, beta pleated sheets and triple helix

34

coil with H bonds between N-H group and O of a C=O in the next turn

alpha helix

35

polypeptides held together side by side by H bonds to make sheets

beta pleated sheet

36

fibrous proteins such as silk

beta pleated sheet

37

hydrogen bonds form between oxygen atoms in the carbonyl groups of one polypeptide chain and the hydrogen atoms in the N-H groups of the amide bonds

beta pleated sheet

38

three polypeptide chains woven together like a braid

triple helix

39

held together by H bonds such as collagen

triple helix

40

most abundant protein in the body

collagen

41

located in fibrous proteins such as wool and hair

tertiary structure

42

helical chains coil together to form a structure like a rope and are held together by S-S bonds

tertiary structure

43

most proteins in the body are made what kind of proteins

globular

44

insulin, hemoglobin, enzymes and antibodies are all what kind of proteins

globular

45

proteins made of polypeptide chains that are folded into different secondary structures that are in turn folded into tertiary structure

globular

46

the tertiary structure of most globular proteins is the active or inactive form

active

47

the globular protein that stores oxygen in skeletal muscles

myoglobin

48

primary structure consists of polypeptide of 153 amino acids

myoglobin

49

tertiary structure is compact shape due to the folding of molecule to form a pocket for O2 to bind

myoglobin

50

the molecule is active only in its tertiary structure

myoglobin

51

tis formed when a globular protein is made of 2 or more peptide chains

quaternary structure

52

the peptide chains can be similar or different and are folded into its secondary and tertiary structure

quaternary structure

53

formed by the binding of the polypeptides in their tertiary structures together

quaternary structure

54

globular protein that transports oxygen to the blood

hemoglobin

55

protein that consists of 4 polypeptide chains or subunits

hemoglobin

56

how should the 4 subunits be held together in hemoglobin

by four different bonds like H bonds and S-S bonds in the quaternary structure

57

bond type of:
primary

peptide

58

bond type of:
secondary

H bonds

59

bond type of:
tertiary

H bonds and S-S bonds

60

bond type of:
quaternary

H bonds and S-S bonds

61

proteins in the primary and secondary structure are active or inactive?

inactive

62

proteins in the tertiary are active if

only one polypeptide is needed

63

proteins in the tertiary are inactive if

more than one polypeptide is needed

64

proteins in the quaternary structure are

active

65

the sequence of amino acids

primary

66

the coiled alpha helix, beta pleated sheet, or a triple helix formed by hydrogen bonding between peptide bonds along the chain

secondary

67

a folding of the protein into a compact, three dimensional shape stabilized by interactions between side R groups of amino acids

tertiary

68

a combination of two or more protein subunits to form a larger biologically active protein

quaternary

69

occurs when the bonds that stabilizes the secondary, tertiary or quaternary are disrupted

denaturation

70

a denatured protein is active or inactive?

inactive

71

denaturation agents

heat (above 50c)
acids and bases disrupt bonds
organic compounds
heavy metal ions
agitation

72

globular proteins that catalyze chemical reactions in the body

enzymes

73

active site is rigid

lock and key model

74

active site is flexible

induced fit model

75

factors affecting enzyme action

substrate concentration
temperature
pH


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