biochemistry Flashcards

1
Q

what is the difference between osmolarity and tonicity?

A

osmolarity is the number of particles in a solution measured in osm/l whilst tonicity considers both the osmolarity of a solution and the osmolarity of the cell

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2
Q

what is the difference between primary and secondary active transport?

A

primary active transport uses energy from ATP e.g. proton pump in the stomach, whilst secondary active transport uses energy from the concentration gradient e.g. the movement of glucose and amino acids into the intestine

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3
Q

what is the equilibrium potential ?

A

where the ions chemical driving force (difference in solute concentration) in one direction = the electrical force (charge difference) in the other direction

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4
Q

what is the resting potential?

A

the difference in electrical potential between the interior and exterior of cell due to large molecules, pumps and channels creating an ion imbalance

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5
Q

what is the main composition of the intracellular fluid?

A

low sodium, high potassium, very low calcium and chloride ions

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6
Q

what is the main composition of the extracellular fluid?

A

high sodium, low potassium, low calcium and chloride

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7
Q

what are the different types of amino acid?

A

electrically charged side chain, uncharged side chain, hydrophobic side chain, and some special cases

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8
Q

what are the features of globular proteins? and two examples

A

compact and usually soluble e.g. enzymes and antibodies

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9
Q

what are the features of fibrous proteins? and 3 examples

A

multiple strands held together by strong bonding

e.g. collagen, keratin, fibroin

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10
Q

what are the features of membrane proteins? and 2 examples

A

hydrophobic regions which sit in the cell membrane e.g. channels and receptors

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11
Q

what causes hyperelastic skin?

A

defect in enzyme procollagen N- proteinase –> malformed fibrils in collagen

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12
Q

what is a prion? and give two examples

A

an infectious protein e.g. BSE, Scrapie

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13
Q

How do enzymes decrease activation energy?

A

bring substrates together, excluding water stabilising transition state, transfer chemical groups

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14
Q

how do isoteric enzymes work?

A

the rate increases with substrate until enzyme is saturated

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15
Q

how do allosteric enzymes work?

A

substrate/ effectors induce a change in the enzyme shape which increases activity - rate increases in a sigmoidal curve

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16
Q

what are the 3 types of allosteric inhibitors?

A

competitive, non competitive ( bind to allosteric site), uncompetitive (bind to E/S complex)

17
Q

list 5 factors which affect enzyme activity

A

temperature, pH, concentration, post transnational modification e.g. phosphorylation, cofactors

18
Q

what is a proteinase? and how are they named?

A

an enzyme which cleaves proteins, they are named after the amino acid at their active site e.g. cysteine proteinase

19
Q

what is a multisubunit enzyme?

A

an enzyme with different forms which can catalyse the same reaction

20
Q

what is a multienzyme complex?

A

an aggregation of several enzymes into a single functional unit