Hemoglobin Flashcards

1
Q

ligand

A

molecule that binds to protein

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2
Q

binding site

A

region in protein where ligand binds

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3
Q

myoglobin

A

binds and stores oxygen in muscle tissue

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4
Q

hemoglobin

A

in red blood cells, transports oxygen and removes carbon dioxide and H+ back to lungs

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5
Q

heme

A

small-molecule porphyrin ring containing iron cation

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6
Q

prosthetic group

A

non-polypeptide unit that forms part of a protein

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7
Q

holoprotein

A

has prosthetic group

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8
Q

apo protein

A

missing prosthetic group

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9
Q

t state

A

deoxygenated, low oxygen affinity

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10
Q

r state

A

open, high oxygen affinity

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11
Q

allostery

A

binding of a ligand at one protein site affects another site allowing for regulation of activity

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12
Q

cooperative binding

A

substrate binding to one subunit changes the likelihood of substrate binding to other subunits

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13
Q

allosteric regulator

A

regulates substrate binding through own interaction with protein at a distance from its catalytic active site

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14
Q

BPG

A

binds and stabilizes central cavity in deoxygenated t state hemoglobin

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15
Q

left shift oxygen curve

A

higher Hb-O2 affinity
lower CO2
higher pH
lower temperature

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16
Q

right shift oxygen curve

A

reduced Hb-O2 affinity
higher CO2
lower pH
higher temperature

17
Q

cellular immune system

A

targets own cells that have been infected
inflammatory T cells

18
Q

humoral immune system

A

targets extracellular pathogens
B-lymphocytes & helper T cells

19
Q

phagocytes

A

cells that eat invaders

20
Q

macrophages

A

large phagocytes that ingest bacteria that are tagged by antibodies

21
Q

antigens

A

stimulate production of antibodies

22
Q

antibodies

A

proteins produced by B cells that bind to antigens

23
Q

induced fit

A

conformation changes upon ligand binding