Drug receptor interactions, Protein and Nucleic acids Flashcards

1
Q

what is this

A

agonist
have affinity and stimulate response

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2
Q

what is this

A

antagonist
have affinity but no response

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3
Q
A

this is an ion gated channel

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4
Q

how does ion gated channels work

A

ionic interaction between CO2 of the receptor and an inducer with NH2Me

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5
Q

How do g-protein coupled receptors work?

A

External messenger that binds to receptor which causes conformational change intracellularly
This change allows binding of a secondary messenger which is cleaved
A part of this molecule will bind to an ezyme to trigger effect

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6
Q

What are the types of agonists

A

full agonist - exert full effects
partial agonist - lesser extent of binding and gives some effect
inverse agonist - exert full reverse effect

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7
Q

What are the different types of antagonist

A

competitive inhibition - bind to active site as per agonist but doesnt cause conformational change

non-competitive inhibition - bind to allosteric binding which causes a conformational change to the active site to prevent agonist binding
umbrella effect - shields binding sites

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8
Q

What are the forces that allow receptor bonding

A

van der waals forces
covalent
ionic
charge transfer bonding - between electron rich and electron dificient
hydrogen bonding
hydrophobic bonding

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9
Q

Describe the structure of a protein

A

consists of amino acids linked by peptide bonds
Usually between COOH and NH2
Are chiral
Can form zwitter ions

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10
Q

What is the primary structure of a protein

A

A sequence of amino acids

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11
Q

What is the secondary structure of a protein

A

Alpha helix
Hydrogen bond every 4th amino acid
rod-like struture
can become superhelix

Beta pleated sheet
H bonding between different primary structures

Beta turn
H bonding between 1st and 3rd amino acid

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12
Q

What is the tertiary structure of a protein

A

Overall 3D structure of polypeptide
contains several bonds between amino acids

hydrophobic
disulfide bridge
ion-dipole
salt bridge
van der waals

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13
Q

What is the quaternary structure of a protein

A

spatial arrangement of protein sub unit

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14
Q

What are some post-translational modifications for proteins

A

N-terminal acetylation
hydroxylation of proline residues
carboxylation of glutamate
phosphorylation og OH
linkage of carbohydrates
cleavage into smaller peptides

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15
Q

What are enzymes

A

they increase rate of reversible bioreactions by lowering activation energy
no influence on reactant concentrations
provides favourable environment - orientates correctly, weaken bonds

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16
Q

What sort of bonding do enzymes undertake

A

ionic bonding
hydrogen bonding
dipole-dipole interactions
Koshlands theory of induced fit - substrate induces active site conformational change

17
Q

What are cofactors

A

Non-protein required to allow for enzyme activity
metal ions or small organic molecules

18
Q

What are the types of enzyme inhibitors

A

competitive, reversible
-bind more strongly than substrate

non competitive, reversible
-allosteric inhibition

non competitive, irreversible
-covalent bonding

19
Q

What is a primary structure of a DNA

A

sequence of RNA chain

20
Q

What is the secondary structure of DNA

A

double helix
antiparallel
stabilised by hydrogen bonding
phosphate outside

21
Q

What do tertiary structure of DNA look like

A

supercoiled helix
by topoisomerase

22
Q

Secondary RNA structure

A

no double helix
some H bonding between nucleobase within one strand