quaternary structure Flashcards

1
Q

how is hemoglobin described

A

tetramer or dimer of alpha beta protomers

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2
Q

how are the subunits of hemoglobin arranged

A

symmetric pairs

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3
Q

what is the individual units that form multimers

A

subunits

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4
Q

what is the individual units that form oligomers

A

protomers

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5
Q

what are the two types of symmetry in protomers

A

rotational and translational

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6
Q

what are the 3 characteristics of guanidinium and urea

A

chaotropic
water solube
disrupt hydrophobic interactions

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7
Q

what is consistent for both the reducing agents of interest

A

thiol group

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8
Q

what are the two reducing agents of interest

A

BME and DTT

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9
Q

what do reducing agents do (2)?

A

reduce disulfide bonds and become oxidized as part of the reaction

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10
Q

how might a protein become locked

A

disulfide bonds reform before removal of denaturant

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11
Q

what kind of process is protein folding

A

cooperative

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12
Q

when does protein assume the molten globule state

A

after formation of secondary but before tertiary

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13
Q

which has more entropy, unfolded or folded

A

unfolded

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14
Q

which has more energy, folded or unfolded

A

foldede

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15
Q

what may assist in protein folding

A

molecular chaperones and isomerases

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