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BIOC3021 > Proteins > Flashcards

Proteins Flashcards

1
Q

A _____ bond is specific to the amide bond in proteins

A

peptide

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2
Q

A peptide bond is between the ____ group of one amino acid and the ____ group of another amino acid

A

carboxyl (COO-), amino (NH3+)

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3
Q

____ is released during a peptide/amide bond formation

A

water

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4
Q

The byproduct of a peptide bond formation is a _______

A

dipeptide

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5
Q

A dipeptide has a ___ end and ____ end

A

N-terminal, C-terminal

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6
Q

The backbone of a dipeptide is repeated _________ units with R side chains

A

N-C alpha-C

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7
Q

The atoms around a peptide bond (CO-NH) are _______

A

coplanar (2D)

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8
Q

_____ is the enzyme that breaks down RNA molecules

A

ribonuclease

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9
Q

The R side chain of the protein is ______

A

hydrophobic

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10
Q

The inside of a protein is ______

A

hydrophillic

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11
Q

______ is a protein that attacks bacterial cell walls

A

lysosine

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12
Q

Every copy of the same protein follows ____ folding patterns

A

the same

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13
Q

Proteins have ____ numbers of chains and disulfide bonds

A

varied

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14
Q

The most abundant protein in humans (25-30% of all proteins) is _____

A

collagen

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15
Q

Collagen is ____ shaped

A

fibrous

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16
Q

Collagen is 1/3 ____ and is rich in _____

A

glycine, proline

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17
Q

A phylogenetic tree compares amino acid sequences of the protein ________

A

cytochrome C

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18
Q

On a phylogenetic tree, amino acid _____ are on the branches

A

changes

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19
Q

_____ proteins require something bound to them to activate

A

conjugated

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20
Q

The binding of nonprotein groups affect protein _____

A

folding

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21
Q

Glyco means ____

A

carbohydrate

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22
Q

Lipo means _____

A

lipid

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23
Q

Nucleo means _____

A

DNA or RNA

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24
Q

Metallo means _____

A

metal ion

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25
Q

Ribonuclease and trypson are examples of what protein function?

A

enzymes (catalyst)

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26
Q

Insulin, trans factor NF-1 are examples of what protein function?

A

regulatory

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27
Q

Hemoglobin and glucose transporter and examples of what protein function?

A

transport

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28
Q

casein and ovalbumin are examples of what protein function?

A

storage

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29
Q

casein and ovalbumin are examples of what protein function?

A

storage

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30
Q

actin, myosin, and tubulin are examples of what protein function?

A

contractile/motile

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31
Q

Collagen and a-keratin are examples of what protein function?

A

structural

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32
Q

Immunoglobulins and fibrinogen are examples of what protein function?

A

protective

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33
Q

Antifreeze and glue proteins are examples of what protein function?

A

exotic

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34
Q

_____ separates ions on the basis of charge

A

chromatography

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35
Q

____ ____ ______ separates ions on the basis of size

A

size exclusion chromatography

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36
Q

_____ _______ separates ions on the basis of affinity (specific binding to small molecules)

A

affinity chromatography

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37
Q

_____ is the movement in an electric field

A

electrphoresis

38
Q

______ separates ions on the basis of molecular weight

A

SDS-PAGE (SDS-polyacrylamide gel electrophoresis)

39
Q

____ _____ separates ions on the basis of isoelectric point (pl)

A

isoelectric focusing

40
Q

pl is a measure of the ____ of the side chain

A

pH

41
Q

____ ___ ____ ______ separates ions on the basis of isoelectric point and molecular weight (added)

A

two dimensional gel electrophoresis

42
Q

___ protein shape is linear molecules that serve structural roles

A

fibrous

43
Q

____ protein shape is a cluster of hydrophobic amino acid insides and hydrophilic amino acid outsides

A

globular

44
Q

_____ protein shape interacts with membrane lipids and has hydrophobic amino acids on the outside

A

membrane

45
Q

collagen is an example of what protein shape?

A

fibrous

46
Q

myoglobin is an example of what protein shape?

A

globular

47
Q

bacteriorhodopsin is an example of what protein shape?

A

membrane

48
Q

What is the first level of protein structure?

A

primary

49
Q

What is the second level of protein structure?

A

secondary

50
Q

What is the third level of protein structure?

A

tertiary

51
Q

What is the fourth level of protein structure?

A

quartenary

52
Q

_____ structure is the amino acid sequence of a protein

A

primary

53
Q

_____ structure is the short range structure in a protein, either alpha helix or beta strand

A

secondary

54
Q

____ structure is the folding of a polypeptide into it’s 3D shape

A

tertiary

55
Q

_____ structure is the numbers and kinds of polypeptide subunits in a protein

A

quaternary

56
Q

_____ structure forms the polypeptide backbone

A

secondary

57
Q

______ structure is the spatial arrangement of polypeptide chains

A

quaternary

58
Q

Ribonuclease is roughly ____ a.a. long

A

124

59
Q

_____ ____/______ are amino acid sequences used repeatedly in a single protein or that are found in different proteins

A

protein domains/modules

60
Q

Protein domains/modules are typically ____ to ____ amino acids long

A

40-100

61
Q

Protein domains do/do not have the same function in different proteins

A

do not

62
Q

What type of protein domain is unusual and less common?

A

different proteins

63
Q

Domains in _____ occur from faulty DNA replication

A

the same protein

64
Q

Domains in ____ occur after the insertion of a copy of a DNA segment into another gene

A

different proteins

65
Q

Some domains are ____ and their function is unknown

A

neutral

66
Q

Domains ____ over time and become unrecognizable to the original

A

mutate

67
Q

A newly synthesized protein first forms segments of ____ _____

A

secondary structure (alpha helix, beta sheets)

68
Q

____ bonding occurs along segments of polypeptides and between segments

A

H

69
Q

Secondary structure of polypeptides arrange into a ______ shape by hydrophobic interactions

A

globular

70
Q

Secondary structure of polypeptides arrange into a globular shape by _______

A

hydrophobic interactions

71
Q

Hydrophobic R side chains want to cluster where?

A

away from water, middle of protein

72
Q

Can secondary structure change during the generation of the tertiary structure?

A

yes

73
Q

Protein folding may need to assistance of ____ _____

A

molecular chaperones

74
Q

What is the role of molecular chaperones?

A

proteins in cell, bind to the new protein and bring parts together to obtain proper 3D folded

75
Q

Do all proteins need molecular chaperones?

A

no

76
Q

___ ____ are misfolded, insoluble, and aggregated proteins in brain cells

A

amyloid deposits

77
Q

What protein is misfolded in Alzheimer’s disease?

A

amyloid-b

78
Q

What protein is misfolded in Parkinson’s disease?

A

a-synuclein

79
Q

____ _____ are protein subunits that combine to form multi-subunit complexes

A

Quaternary structures

80
Q

Proteins can have either ____ subunits or _____ types of protein chains

A

identical, different

81
Q

The ______ produces quaternary structure are the same as those used for tertiary structure

A

forces

82
Q

What 4 things play a role in quaternary structure production?

A

hydrophobic interactions, hydrogen bonding, ionic interactions, disulfide bonds

83
Q

Quaternary structure allows for _____ _____ between protein subunits

A

cooperative behavior

84
Q

In hemoglobin, there are ____ protein subunits

A

4

85
Q

How does hemoglobin exhibit cooperative behavior?

A

The binding of the first O2 molecule makes it easier for the other 3 O2 molecules to bind to the protein subunits

86
Q

Hemoglobin aides in what physiological function?

A

rapid release of O2 into lungs

87
Q

What are the two types of quaternary structure?

A

fixed number, open

88
Q

What are microtubules?

A

long, hollow tubes

89
Q

Where are microtubules found?

A

cytoskeleton (cell structure), mitotic spindles (cell division process)

90
Q

Tubulin dimers _____ to form microtubules

A

polymerize

91
Q

Microtubules are dynamic and can easily ______

A

increase or decrease in length

92
Q

Microtubules have ____ quaternary structure

A

open

BIOC3021 (25 decks)

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