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Biomedicine Specialised Core Subjects > Proteins > Flashcards

Proteins Flashcards

(75 cards)

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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
What holds proteins shape
H bonds, Van Der waals attraction and electrostatic attraction
26
What is the primary structure
Order of amino acids from the NH3+ end to the O- end
27
What is secondary structure
Repeating patterns stabilised by weaker bonds
28
What is tertiary structure
Overall conformation
29
What is quaternary structure
Interaction of multiple subunits (single chains)
30
What are alpha helixes and beta pleated sheets stabilized by
H bonds
31
Why are genetic defects catastrophic
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
What is a domain
stable substructure of proteins
33
What is a transmembrane protein
A nonpolar protein that hangs around within the cell membrane
34
What is a property of beta pleated sheets
High tensile strength, used for silk and spider webs
35
Do all genetic mutation which change primary structure change function
No
36
What are the types of disuplhide bridges?
Inter and intrachain
37
What is a simple protein
Proteins with only amino acids
37
What is a conjugated protein
Proteins with other stuff as well as amino acids
37
What is a lipoprotein
Conjugated protein with a lipid
38
What is a metalloprotein
Conjugated protein with a metal
39
What is a glycoprotein
Conjugated protein with sugar groups
40
What is a prosthetic group
A group that isn't an amino acid in a protein.
41
What is a coordinate bond
metals can receive 2 electrons from a nonmetal donor which forms a coordinate bond
42
How are protein relationships detrmined
By similarity of amino acid sequences
43
What is protein conformation
Protein shape
44
What does destroying the conformation do to a protein
Denature
45
How do we denature a protein
By breaking disulphide bridges, hydrogen bonds, van der walls and dipole dipole forces
46
How do eggs fry
By denaturing ovalbumin
47
Is denaturing reversible
Probably not, but if it doesn't change the primary structure yes
48
How do we break hydrogen bonds, dipole dipole and dispersion bonds
By adding heat or chemicals depeniding on how easy it is to denature
49
What are the types of proteins
Transport proteins Storage proteins Protective proteins Motile proteins (muscle)
50
What can H bonds be denatured by
Heating
51
What can S-S bonds be denatured by
Strong Reducing agents
52
What can detergents denature
Hydrophobic regions
53
What influences function
shape
54
What is an example of a (usually) globular protein
Enzymes
55
What is something that binds to a protein
Ligand
56
What are ligands usually bound by
Noncovalent bonds
57
What does an enzyme do
Enzyme binds specific ligands (substrates). It alters its configuration so it can be converted into a product rapidly
58
Where does a reaction take place in an enzyme
Active site
59
How much do enzymes speed up reaction rate
LOTS from twice per minute to hundreds of thausands of molecuels per second
60
What are metabolic pathways
Chain of reactions catylysed by enzymes
61
How do you change proteins shape by one simple ion
Adding phosphates
62
Why are phosphates important for enzymes
Because a phosphate might turn an enzyme on and off by changing the shape.
63
What is a kinase enzyme
Adds phosphate from enzymes
64
What is a phosphatase enzyme
Removes phosphate from enzymes
65
What does enzymes always end with
ASE
66
What is ligase
Catalyse formation of bonds
67
What is a polymerase
Catalyze polymerisation reactions
68
What is a protease
Break peptide bonds in proteins
69
What is a oxidoreductase
Catalyze redox reactions
70
what is transferase
Catylyzes transfer of groups
71
What is a redox reaction
Where electrons transfer
72
What do electrons usually transfer with in the cell
H or H-
73

Biomedicine Specialised Core Subjects (20 decks)

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