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FUN biomed and pharmo > FUN2/Proteins > Flashcards

FUN2/Proteins Flashcards

1
Q

In an amino acid, what determines the chemical properties?

A

side-chain/r group

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2
Q

once inserted into a _____, amino acid properties determine how they will behave

A

polypeptide chain

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3
Q

What are all the essential amino acids?

A

PVT TIM G. HALL
phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, (glutamine - critically ill) histidine, arginine (children) lycine, and leucine

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4
Q

What does Private Tim G. Hall LIV for?

A

the branches, (leucine, isoleucine, and valine)

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5
Q

Where does private time g hall live?

A

Basic training HAL (histidine, arginine, lysine)

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6
Q

Which is the smallest r group?

A

glycine

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7
Q

Which of the amino acids are hydrophobic?

A

IMPACT GVLP

A-Alanine, T-tryptophan, G-Glycine, L-Leucine

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8
Q

What of the amino acids are hydrophilic?

A

STALAG GHAT

T-Tyrosine Threonine, A-Asparagine, Aspartic Acid, Arginine, L-Lycine, G-Glutamic Acid, Glutamine

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9
Q

What do all of the charged amino acids have in common?

A

they are all hydrophilic

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10
Q

Does alanine fold easily or difficultly?

A

easily

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11
Q

Which of the amino acids are negatively charged?

A

GA(glutamic and aspartic)

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12
Q

which of the amino acids are positivly charged?

A

HAL(histidine, arginine, and lysine)

private tim g hall has a POSITIVE experience living in the BASIC training hall

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13
Q

What type of group does Tyrosine have on it?

A

hydroxyl group

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14
Q

True or false? Tyrosine can be phosphorylated?

A

true

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15
Q

In tryptophan, the main part is considered hydro_____, but can be considered slightly hydro______ because of the ___?

A

phobic, philic, N

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16
Q

Asparagine interacts with a ______?

A

carbohydrate

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17
Q

What is the interaction with a carbohydrate called?

A

glycosylation

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18
Q

How many amino acids contain sulphur atoms and what are they?

A

2, Cystine and methionine

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19
Q

What type of bonds is cystine involved in?

A

disulphide bonds

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20
Q

What type of amino acid is proline?

A

imino amino acid

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21
Q

Which amino acid is found at bends and turns in protein structure?

A

proline

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22
Q

What type of reaction is used to form a peptide bond?

A

condensation reaction, dehydration reaction

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23
Q

What is the basic chemical formula for a peptide bond?

A

C(O)NH

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24
Q

The start of a polypeptide chain is called the _____ terminus, and the end of a polypeptide chain is called the _____ terminus.

A

amino (N), carboxyl (C)

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25
Q

What does native conformation mean?

A

3-D structure

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26
Q

What structure does native conformation start at?

A

secondary

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27
Q

What are the 2 types of secondary structures?

A

alpha helix and beta pleated sheet

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28
Q

The alpha helix is stablized by ______ bonds between every _____ (number) amino acid.

A

hydrogen, fourth

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29
Q

The hydrogen bonds form between what groups?

A

CO1- and NH1+

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30
Q

Can the alpha helix structure be predicted?

A

yes

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31
Q

How many amino acid residues are there in a 360 degree turn of the helix?

A

3.6

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32
Q

Do the hydrogen bonds in the beta pleated sheet form adjacent or away from each other?

A

adjacent

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33
Q

What are the 2 ways adjacent chains in a beta pleated sheet can run?

A

parallel and antiparallel

34
Q

ex. of alpha helix

A

collagen and keratin in hair

35
Q

ex. of beta pleated sheet

A

silk

36
Q

When a protein folds into tertiary structure what form does it take?

A

globular

37
Q

What determines the tertiary structure?

A

aa sequence

38
Q

There are ____ (more/less) distant interactions within proteins in tert. structure

A

more

39
Q

What type of interactions are hydrogen bonds?

A

electrostatic

40
Q

A disulphide bond is formed from a reaction of 2 ______.

A

cyteines

41
Q

What 2 things controls folding in a protein?

A

aa seq and disulphide bonds

42
Q

A peptide bond is a partial ____ bond?

A

double

43
Q

What are 2 characteristics of a peptide bond?

A

rigid and planar

44
Q

is there a lot or a little bit of rotation in a peptide bond?

A

very limited

45
Q

A peptide bond has what type of configuration?

A

trans

46
Q

what is a trans configuration in a peptide bond?

A

alpha carbons are opposite to each other

47
Q

how many polypeptide chains does Quaternary structure consist of at least?

A

2

48
Q

in Quaternary structure do they polypeptide chains have to be the same or do they have to be different?

A

does not matter, they can be the same or diff

49
Q

What holds the Quaternary structure together?

A

noncovalent interactions and interchain disulphide bonds

50
Q

ex. of globular proteins

A

myoglobin

51
Q

Are globular proteins compact or loose?

A

compact

52
Q

in globular proteins the hydrophobic aa’s are on the_____

A

inside

53
Q

in globular proteins the hydrophilic aa’s are on the_____

A

outside

54
Q

in globular proteins the _______ aa’s are on the inside

A

hydrophobic

55
Q

in globular proteins the _____ aa’s are on the outside

A

hydrophilic

56
Q

What 4 things stabilize globular proteins?

A

disulphide bonds
hydrophobic interactions
hydrogen bonds
ionic interactions

57
Q

globular proteins are a combination of _____ structure elements?

A

secondary

58
Q

regions in globular proteins are connected by _______

A

loops/alpha helix

arrows/beta pleated sheet

59
Q

super-secondary structures are called_____

A

domains/motifs

60
Q

ex. of beta pleated sheet BARREL

A

porin

61
Q

what is the function of porin?

A

forms pores in the cell membrane

62
Q

what is the structure of fibrous proteins?

A

it is a long rigid structure where 3 polypeptides are wound like a rope-like triple helix

63
Q

what aa’s are rich in fibrous proteins?

A

proline and glycine

64
Q

proline and lysine residues are _______ated?

A

hydroxylated

65
Q

What are the processes of protein structure?

A

assembly, folding, packing, interaction

66
Q

name some functions of a protein once it is in native conformation (6)

A

catalysis, protection, regulation, signal transduction, storage, transport

67
Q

what kind of modification happens in post translational modification? (PTM)

A

chemical

68
Q

what is attached to the amino acid in PTM, and what happens to the entire protein after that

A

a functional (R) group, changed the protein’s function

69
Q

PTM: phosphorylation

A

add phosphate onto serine, threonine, tyrosine

70
Q

PTM: glycolsylation

A

add sugar group onto asparagine, serine, threonine

71
Q

PTM: acylation

A

add fatty acid on N termini onto serine, alanine, methionine, glycine, and threonine

72
Q

PTM: ubiquitination

A

add ubiquitin onto lysine, serine, threonine, cysteine

73
Q

PTM: nitrosylation

A

add nitric oxide onto cysteine

74
Q

what is ubiquitin

A

helps in the destruction of defective proteins

75
Q

a deficiency of enzymes in the _________ ________ pathway can cause abnormal glycosylation which can interfere with proper metabolism

A

oligosaccharide synthetic

76
Q

go over some context CDG

A

protein ppt

77
Q

when protein aggregation is abnormal, the ______ are misfolded

A

fibrils

78
Q

ex. of a fibril

A

amyloid

79
Q

amyloid can be formed from ______ (number) proteins

A

over 20

80
Q

ex. of abnormal protein aggregation/misfolded proteins in brain

A

alzheimers diesease

FUN biomed and pharmo (8 decks)

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