Notes in h. Protein Conformation and Function (Hemoglobin)

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Published	07/28/2024	The structures of myoglobin and hemoglobin are composed primarily of {{c1::alpha helices}} [ Hint: secondary structure]
Published	07/28/2024	Fe(II) in Heme is coordinated by what 5 factors?
Published	07/28/2024	Hb Fe(II) can be oxidized to Fe(III) resulting in {{c1::metHb}}
Published	07/28/2024	metHb preferentially binds {{c1::H2O}}
Published	07/28/2024	The enzyme {{c1::metHb (cytochrome b5 reductase)}} reverses the inactivation of Hb by converting Fe(III) back to Fe(II)
Published	07/28/2024	The binding of oxygen to myoglobin follows a {{c1::hyperbolic}} curve
Published	07/28/2024	The binding of oxygen to hemaglobin occurs with a {{c1::sigmoidal}} curve
Published	07/28/2024	The {{c1::distal histidine}} is a gatekeeper that prevents superoxide from leaving the active site
Published	07/28/2024	The conversion of oxygen to superoxide when bound to heme causes the formation of {{c1::metHb}}
Published	07/28/2024	The ideal hill coefficient for hemoglobin is {{c1::4}}
Published	07/28/2024	In reality, the hill coefficient for hemoglobin is {{c1::2.8}}
Published	07/28/2024	Quaternary structure of deoxyHb is referred to as the {{c1::T (tense)}} state
Published	07/28/2024	Quaternary structure of oxyHb is referred to as the {{c1::R (relaxed)}} state
Published	07/28/2024	2,3-BPG is released from Hb during the {{c1::T-to-R transition}}
Published	07/28/2024	Fetal hemaglobin utilizes {{c1::alpha-gamma}} subunits to better bind maternal oxygen from the placenta
Published	07/28/2024	A {{c1::decrease}} in pH {{c2::increases}} Hb oxygen delivery
Published	07/28/2024	A {{c1::increase}} in CO2 {{c2::increases}} Hb oxygen delivery
Published	07/28/2024	Stabilizing the {{c1::T}} state of Hb is important for releasing O2
Published	07/28/2024	What allosteric effectors stablize the T state of Hg in order to increase the release of O2?
Published	07/28/2024	Carbonic anhydrase has {{c1::Zn2+}} cofactor in its active site
Published	07/28/2024	{{c1::Thalassemias}} are caused by the loss or reduction of either the alpha or the beta subunits of Hb
Published	07/28/2024	{{c1::Hemoglobinopathies}} are caused by single mutations in the primary structure of the alpha or beta subunits in Hb
Published	07/28/2024	The most common hemoglobinopathy is {{c1::sickle cell anemia}}
Published	07/28/2024	Thalessemia are caused by {{c1::improper mRNA splicing}}
Published	07/28/2024	What causes the pathology of sickle cell anemia?
Published	07/28/2024	What does the hydroxyurea treatment do in the treatment of sickle cell anemia?
Published	07/28/2024	What is the A1C level?
Published	07/28/2024	In the case of hypoxia, the hypoxia response element is activated, causing transcription of proteins responsible for?
Published	07/28/2024	Hemoglobin (Hb) transports {{c1::O2}} from the lungs to tissues, transports {{c1::CO2}} from tissues to lungs, and transports {{c1::NO}} (a vasodilato…
Published	07/28/2024	Three molecules that bind Hb with greater affinity than O2 are -
Published	07/28/2024	The last O2 in Hb binds {{c1::100 times more}} tightly than first O2
Published	07/28/2024	How does cooperativity occur in Hb?
Published	07/28/2024	2,3-BPG lies in the pocket present in {{c1::T}} state. This pocket is surrounded by {{c1::positively}} charged residue
Published	07/28/2024	In fetal Hb, {{c1::His143}} of the adult ß chain, part of the 2,3-BPG binding site, is replaced by {{c1::Ser}}.This {{c1::reduces}} affinity for 2,3-B…
Published	07/28/2024	At low pH {{c1::His 146}} is protonated which stabilizes {{c1::T}} state
Published	07/28/2024	Both bicarbonate and carbamate formation stabilize {{c1::T}} state over {{c1::R}} state because they are derived from excess carbon dioxide, causing r…
Published	07/28/2024	A1C Level Normal below {{c1::5.7}} percent Prediabetes {{c1::5.7 to 6.4}} percent Diabetes {{c1::6.5}} percent or above
Published	07/28/2024	How does HIF1a respond to normoxia and hypoxia?
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