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Biomedicine Specialised Core Subjects > Proteins > Flashcards

Proteins Flashcards

1
Q

What is the central dogma

A

DNA can replicate itself which produce our genetic codes. DNA then can turn into RNA and then into proteins so proteins are genetically coded.

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2
Q

What is the monomer of proteins

A

Alpha amino acids

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3
Q

What is required for an organic molecule to become an alpha amino acid

A

There is a amine group, a carboxyllic acid group, a hydrogen atom and an r group attached to the central alpha carbon.

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4
Q

What is on the left end and what is on the right end on the primary structure of all proteins

A

Left end - Amino
Right end - Carboxuyllic acid

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5
Q

What are the basic amino acids

A

Lysine
Arganine
Histidine

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6
Q

What are the acidic amino acids

A

Aspartic acid
Glutamic acid

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7
Q

What makes a basic side chain

A

NH3+ ion on the chain

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8
Q

What makes an acidic side chain

A

O- ion on the chain

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9
Q

What has a H side chain

A

Glycine

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10
Q

What has a methyl side chain

A

Alanine

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11
Q

What has a phenyl and methyl side chain

A

Phenylalanine

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12
Q

What has a phenyl a methyl and a hydroxyl side chain

A

Tyrosene

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13
Q

What is chirality

A

Where there are four unique chains on a carbon

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14
Q

What orientation is bacterial amino acids

A

D amino acids

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15
Q

What orientation is Human amino acids

A

L amino acids

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16
Q

Why is orientation important for proteins

A

Proteins are catalyzed by enzymes, which have holes for specific orientations, if you have the wrong orientation it won’t catalyze.

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17
Q

What form do amino acids exist in water

A

Zwitterions (NH3+ and COO-)

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18
Q

What is amphoteric

A

Acids and bases simultaneously

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19
Q

Why are amino acids somewhat insoluble water

A

Because the ions are attracted to each other rather than water

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20
Q

What is the isoelectric point

A

PH Point where it is least soluble in water, most atoms are zwitterions

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21
Q

What does water do to protein shape

A

This allows hydrophillic parts of the protein to go near the water and go outside and hydrophobic parts of the protein in the middle

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22
Q

How are proteins polymerised

A

Through peptide bonds via condensation

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23
Q

Why are peptide bonds inflexible

A

Because it has a partial double bond configuration

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24
Q

What is a disulphide bond

A

A covalent bond in between proteins which is forms with oxidation between two cystine amino acids

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25
Q

What holds proteins shape

A

H bonds, Van Der waals attraction and electrostatic attraction

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26
Q

What is the primary structure

A

Order of amino acids from the NH3+ end to the O- end

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27
Q

What is secondary structure

A

Repeating patterns stabilised by weaker bonds

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28
Q

What is tertiary structure

A

Overall conformation

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29
Q

What is quaternary structure

A

Interaction of multiple subunits (single chains)

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30
Q

What are alpha helixes and beta pleated sheets stabilized by

A

H bonds

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31
Q

Why are genetic defects catastrophic

A

DNA forms proteins and if DNA is defected, then primary structure of protein is changed and then function is changed making the protein do the wrong function

32
Q

What is a domain

A

stable substructure of proteins

33
Q

What is a transmembrane protein

A

A nonpolar protein that hangs around within the cell membrane

34
Q

What is a property of beta pleated sheets

A

High tensile strength, used for silk and spider webs

35
Q

Do all genetic mutation which change primary structure change function

A

No

36
Q

What are the types of disuplhide bridges?

A

Inter and intrachain

37
Q

What is a simple protein

A

Proteins with only amino acids

37
Q

What is a conjugated protein

A

Proteins with other stuff as well as amino acids

37
Q

What is a lipoprotein

A

Conjugated protein with a lipid

38
Q

What is a metalloprotein

A

Conjugated protein with a metal

39
Q

What is a glycoprotein

A

Conjugated protein with sugar groups

40
Q

What is a prosthetic group

A

A group that isn’t an amino acid in a protein.

41
Q

What is a coordinate bond

A

metals can receive 2 electrons from a nonmetal donor which forms a coordinate bond

42
Q

How are protein relationships detrmined

A

By similarity of amino acid sequences

43
Q

What is protein conformation

A

Protein shape

44
Q

What does destroying the conformation do to a protein

A

Denature

45
Q

How do we denature a protein

A

By breaking disulphide bridges, hydrogen bonds, van der walls and dipole dipole forces

46
Q

How do eggs fry

A

By denaturing ovalbumin

47
Q

Is denaturing reversible

A

Probably not, but if it doesn’t change the primary structure yes

48
Q

How do we break hydrogen bonds, dipole dipole and dispersion bonds

A

By adding heat or chemicals depeniding on how easy it is to denature

49
Q

What are the types of proteins

A

Transport proteins
Storage proteins
Protective proteins
Motile proteins (muscle)

50
Q

What can H bonds be denatured by

A

Heating

51
Q

What can S-S bonds be denatured by

A

Strong Reducing agents

52
Q

What can detergents denature

A

Hydrophobic regions

53
Q

What influences function

A

shape

54
Q

What is an example of a (usually) globular protein

A

Enzymes

55
Q

What is something that binds to a protein

A

Ligand

56
Q

What are ligands usually bound by

A

Noncovalent bonds

57
Q

What does an enzyme do

A

Enzyme binds specific ligands (substrates). It alters its configuration so it can be converted into a product rapidly

58
Q

Where does a reaction take place in an enzyme

A

Active site

59
Q

How much do enzymes speed up reaction rate

A

LOTS from twice per minute to hundreds of thausands of molecuels per second

60
Q

What are metabolic pathways

A

Chain of reactions catylysed by enzymes

61
Q

How do you change proteins shape by one simple ion

A

Adding phosphates

62
Q

Why are phosphates important for enzymes

A

Because a phosphate might turn an enzyme on and off by changing the shape.

63
Q

What is a kinase enzyme

A

Adds phosphate from enzymes

64
Q

What is a phosphatase enzyme

A

Removes phosphate from enzymes

65
Q

What does enzymes always end with

A

ASE

66
Q

What is ligase

A

Catalyse formation of bonds

67
Q

What is a polymerase

A

Catalyze polymerisation reactions

68
Q

What is a protease

A

Break peptide bonds in proteins

69
Q

What is a oxidoreductase

A

Catalyze redox reactions

70
Q

what is transferase

A

Catylyzes transfer of groups

71
Q

What is a redox reaction

A

Where electrons transfer

72
Q

What do electrons usually transfer with in the cell

A

H or H-

73
Q
A

Biomedicine Specialised Core Subjects (20 decks)

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