Notes in L7 - Hemoglobin/Myoglobin Structure + Function

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Status	Last Update	Fields
Published	11/02/2024	what is the trend for curve shift and hb conformation
Published	11/02/2024	What factors increase hemoglobin unloading (right shift)?{{c1::increased}} 2,3 BPG{{c1::increased}} H+{{c1::increased}} pCO2{{c1::decreased}} O2 …
Published	11/02/2024	What factors lead to a left shift in the oxygen-hemoglobin dissociation curve?The following favor the {{c1::R}} conformation of hemoglobin:{{c1::high}…
Published	11/02/2024	The {{c1::first}} O2 molecule is the most difficult to bind to hemoglobin.
Published	11/02/2024	Deoxyhemoglobin is characterized as being in the {{c1::taut (T)}} conformation and possessing a {{c1::low}} affinity for O2
Published	11/02/2024	Oxyhemoglobin is characterized as being in the {{c1::relaxed}} state and has a {{c1::high}} affinity for oxygen
Published	11/02/2024	The pO2 of tissues and lungs are roughly {{c1::30}} mmHg and {{c1::100-120}} mmHg respectively
Published	11/02/2024	Increases in 2,3 BPG at high altitudes is critical for {{c1::the proper unloading of O2 at tissues}}
Published	11/02/2024	Heme is {{c1::an organic cofactor}} while hemoglobin is a {{c1::hemeprotein}}
Published	11/02/2024	hemoglobin {{c1::transports O2 to tissues::function}} while myoglobin {{c1::stores O2 in resting muscle and releases it after muscle contraction::func…
Published	11/02/2024	the tertiary structure of myoglobin and hemoglobin are stabilized by {{c1::hydrophobic interactions}}
Published	11/02/2024	2 basic {{c1::histidine}} residues are involved in heme binding: - {{c1::F8}} binds heme Fe2+- {{c1::E7}} stabilizes O2 binding
Published	11/02/2024	hemoglobin is water {{c1::soluble::soluble/insoluble}}
Published	11/02/2024	hemoglobin is a {{c1::tetramer comprised of 2 α and 2 β globin chains::structure}}myoglobin is a {{c1::monomer::structure}}
Published	11/02/2024	Weak {{c1::ionic}} and {{c1::hydrogen}} bonds hold the two dimers of hemoglobin together
Published	11/02/2024	In hemoglobin:Each globin subunit covalently binds the {{c1::Fe2+ iron in heme}}Each heme molecule can bind {{c1::O2}} , and this induces a conformati…
Published	11/02/2024	O2 is a {{c1::positive homotropic effector}} of Hb
Published	11/02/2024	485edbdd66794c2b8cf227fa622594d9-ao-1
Published	11/02/2024	485edbdd66794c2b8cf227fa622594d9-ao-2
Published	11/02/2024	how is O2 replenished during muscle contraction?{{c1::During muscle contraction, O2 is consumed by mitochondria to produce ATP, so O2 levels become de…
Published	11/02/2024	P50 value is the {{c1::partial pressure of O2 (pO2 ) at which a molecule is 50% saturated with O2}}
Published	11/02/2024	Two major metabolic pathways, the {{c1::citric acid cycle}} and the {{c1::glycolytic pathway}}, indirectly modulate the binding and release of O2…
Published	11/02/2024	how does CO2 from the CAC act as a negative effector on hemoglobin in tissues?
Published	11/02/2024	how does CO2 in the lungs affect pH and Hb affinity for O2?
Published	11/02/2024	the {{c1::Bohr effect}} explains how increased [H+] and pCO2 decrease O2 binding to Hb
Published	11/02/2024	explain how CO2 can directly affect Hb affinity in tissues and in lungs
Published	11/02/2024	2,3-BPG preferentially binds and stabilizes {{c1::deoxyHb}} and favors the {{c1::T}} state
Published	11/02/2024	less 2,3-BPG means {{c1::less}} O2 will be released to tissuesmore 2,3-BPG means {{c1::more}} O2 will be released to tissues
Published	11/02/2024	CO binds to the Fe2+ ion in Hb with {{c1::220X greater}} affinity than O2 to form {{c1::Carbon monoxyhemoglobin}}
Published	11/02/2024	explain why CO is toxic to humans
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