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biochem lec > organization structure of proteins > Flashcards

organization structure of proteins Flashcards

1
Q

sequencce of amino acids

A

primary structure

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2
Q

it gives identity to protein

A

sequence of amino acids

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3
Q

what are the structures?

A

primary, secondary, tertiary, quaternary

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4
Q

alpha-helix, beta-pleated sheet, triple helix

A

secondary structure

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5
Q

simple molecules

A

quaternary structure

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6
Q

how many molecules in hemoglobin

A

four (2 alpha and 2 beta)

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7
Q

hemoglobin has this structure that binds to what?

A

hemistructure; iron (gives capacity as oxygen transporter)

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8
Q

it affects other levels of protein structural organization

A

primary structure

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9
Q

primary structure involves only the ______ linking residues together

A

covalent bonds

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10
Q

the minimum size of a protein is defined as about ____ residues; smaller chains are referred to simply as _____. So the primary structure of a small protein would consist of a sequence of ____ or so residues

A

50; peptides; 50

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11
Q

how many molecular weight per residue?

A

110 Da (daltons)

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12
Q

largest protein discovered has how many residues and daltons/mweight?

A

30k residues and 3 million Da

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13
Q

insulin has how many amino acids?

A

51

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14
Q

what is the linkage for cysteine to cysteine?

A

disulfide linkage

  • intramolecular if within one amino only
  • intermolecular if with another amino acid
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15
Q

largest known protein

A

titin or connectin

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16
Q

is found in the striated muscle tissue of humans and other vertebrates

A

titin or connectin

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17
Q

human titin is >1 µm long and consists of ___ folded protein domains

A

244

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18
Q

Adults’ bodies contain ≈ __ g of titin.

A

500g

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19
Q

who identified the sequence of insulin?

A

frederick sanger

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20
Q

insulin has how many disulfide linkages?

A

three (1 intra and 2 inter)

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21
Q

what is the structure of insulin?

A

tertiary structure

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22
Q

the ____ structure of proteins can be characterized as a regular _____ structure held together by _____ bonding between the O of the___ and the H of the ____ groups in the polypeptide chains

A

secondary; three-dimensional, hydrogen, carbonyl (C=O), amino (NH)

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23
Q

two examples of secondary structure

A

a-helical and b-pleated-sheet structures

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24
Q

shape or conformation of a protein molecule

A

tertiary structure

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25
Q

combination of secondary structure

A

tertiary structure

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26
Q

what are the interactions in tertiary structure?

A

disulfide bonding
hydrogen bonding
ionic bonding
hydrophobic attractions

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27
Q

known also as the salt-bridge

A

ionic bonding

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28
Q

positive ionic bonding is

A

basic amino acids (Arg, Lys, His)

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29
Q

negative ionic bonding

A

acidic amino acids (aspartic and glutamic acids)

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30
Q

nonpolar amino acids have what

A

hydrophobic attractions

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31
Q

attraction between negatively and positively charged substituents on the R-groups

A

ionic bonding

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32
Q

electrostatic attractions between COO- and N+ on acidic and basic side groups

A

ionic bonding

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33
Q

Can occur between side chains that contain a hydrogen donor

A

hydrogen bonding

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34
Q

occurs between a residue with an OH or NH and a residue with C = O, COOH, OH or NH

A

hydrogen bonding

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35
Q

May be intermolecular of intramolecular

A

hydrogen bonding and disulfide linkage

36
Q

Can form between the –SH groups of two cysteine amino acids

A

disulfide linkages

37
Q

greater attraction than h-bonding

A

disulfide linkages

38
Q

Can exist between the Rgroups of nonpolar amino acid residues

A

hydrophobic attractions

39
Q

what is the bond in disulfide linkages

A

covalent bond

40
Q

a misnomer

A

hydrogen bonding

41
Q

in aqueous media, the chain folds so that the hydrophobic side chains face toward the interior, away from the outside environment of polar water molecules

A

hydrophobic attractions

42
Q

the hydrophobic groups associate together, strengthening the attractive dispersion forces and minimizing the possibility of a water molecule coming between them

A

true

43
Q

hydrogen bonding only occurs in?

A

O to H

44
Q

it determines the tertiary structure of insulin

A

disulfide bonding

45
Q

to manipulate the tertiary structure of hair protein

A

redox reaction

46
Q

loss of hydrogen, loss of electron, gain of oxygen

A

oxidation

47
Q

gain of hydrogen, gain of electron, loss of oxygen

A

reduction

48
Q

it breaks down disulfide linkages

A

reducing agent

49
Q

it binds the disulfide linkages again

A

oxidizing agent

50
Q

some complex proteins with two or more polypeptide chains can have what is known as __________

A

quaternary structure

51
Q

same forces and bonds that create tertiary structure also hold subunits together (quaternary) in a stable complex to form the _____ protein

A

complete protein

52
Q

some proteins are composed of more than one polypeptide chain

A

quaternary structure

53
Q

refers to the number and arrangement of the individual polypeptide chains

A

quaternary structure

54
Q

each polypeptide is referred to as a ______ of the protein

A

subunit

55
Q

_______ is a tetramer containing two pairs of non-identical (but similar) subunits. It has 2 α subunits and 2 β subunits

A

hemoglobin

56
Q

substance inside red blood cells that binds to oxygen in the lungs and carries it to the tissues (contains iron)

A

heme

57
Q

classify the bonds in each protein structure

A

primary: covalent bond
secondary: hydrogen bonding
tertiary and quaternary: hydrogen bonding, disulfide linkages, ionic bonding, and/or hydrophobic attraction

58
Q

are proteins that have a fiber-like shape

A

fibrous proteins

59
Q

Fibrous proteins serve as _____ supports and tend to be water ________

A

structural, insoluble

60
Q

a fibrous protein found in tendons, ligaments, and bone matrix

A

collagen

61
Q

what bond holds a-keratin?

A

disulfide bonding/linkage

62
Q

keratin is a ___ protein

A

fibrous

63
Q

fibroin forms what?

A

silk (fibroin is also a fibrous protein)

64
Q

proteins where the polypeptide chains are folded in a spherical or globular shape

A

globular proteins

65
Q

Globular proteins tend to be water ____- and can act as binding agents, enzymes, and as transport vehicles within the ___

A

soluble, binding agents, enzymes, transport vehicles, blood

66
Q

what are the four important globular proteins?

A

carboxypeptidase A, myoglobin, hemoglobin, immunoglobulin G

67
Q

myoglobin functions as a binding protein carrying _____ for muscle tissue

A

oxygen

68
Q

small enzyme that catalyzes protein digestion in the small intestine

A

carboxypeptidase A

69
Q

these proteins bind molecules that are foreign to the body, as a defense against disease

A

immunoglobulin g

70
Q

heme is a what group?

A

a prosthetic group

71
Q

present in proteins that have oxygen

A

heme

72
Q

oxygen-hemoglobin binding process, amount of oxygen/s in the cycle

A

0 1 4 3

0 starting, 1 will add
1 added, 3 more adds (oxygen binding)
4 added, 1 will remove
3 present, 3 will be released

73
Q

Some proteins contain polypeptide molecules associated with molecules or ions other than polypeptides

A

conjugated proteins

74
Q

hemoglobin includes the molecule ____ and the ion ____ in addition to the polypeptide molecule

A

heme and Fe2+ (iron)

75
Q

nonpolypeptide molecules are referred as what?

A

prosthetic groups

76
Q

proteins containing prosthetic groups are

A

conjugated proteins

77
Q

proteins without prosthetic groups are

A

simple proteins

78
Q

good cholesterol

A

high density lipoprotein (lipid carrier)

79
Q

what are the different classes in conjugated proteins?

A

glycoprotein, lipoprotein, nucleoprotein, hemoprotein, metalloprotein, phosphoprotein

80
Q

gamma globulin, mucin, interferon

A

glycoprotein

81
Q

hemoglobin, myoglobin

A

hemoprotein

82
Q

vldl, ldl, hdl

A

llipoprotein

83
Q

fe and zn

A

metalloprotein

84
Q

rna-bound protein

A

nucleoprotein

85
Q

casein

A

phosphoprotein

biochem lec (5 decks)

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