Notes in Hemoglobin

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Status	Last Update	Fields
Published	09/07/2023	{{c1::Quaternary structure}} is formed by the assembly of individual polypeptides (subunits) into a larger functional cluster.
Published	09/07/2023	What is allostery?
Published	09/07/2023	Allostery results in what kind of protein modifications?{{c1::modifying the protein structure or conformational preferences modying charge distri…
Published	09/07/2023	True or false: Allostery is typically associated with multisubunit proteins
Published	09/07/2023	Hemoglobin is a dimer of {{c1::dimers}}
Published	09/07/2023	Hb has a {{c1::T}} state (lacks O2) and an {{c1::R}} state (binds O2)
Published	09/07/2023	Oxygen binding on Hb is {{c1::reversible}} and {{c1::cooperative}}
Published	09/07/2023	HbF (Fetal) is composed of 2 {{c1::gamma}} globins + 2 {{c1::alpha}} globins
Published	09/07/2023	Adult hemoglobin (HbA) is composed of 2 {{c1::alpha}} globin and 2 {{c1::beta}} globin chains
Published	09/07/2023	{{c1::HbA}} has an all helical structure, called the {{c1::globin}} fold
Published	09/07/2023	Hb contains a {{c1::heme}} (iron-containing) cofactor; iron (Fe2+) is ligated by {{c2::histidines}}
Published	09/07/2023	Hb exhibits {{c1::cooperativity}}, in that binding of O2 on one subunit increases other subunits' O2 affinity
Published	09/07/2023	{{c1::O2}} binding to Hb causes movement of iron atom, which alters protein conformation
Published	09/07/2023	The two models for Hb T to R state transition are: {{c1::concerted}} (shifting equilibrium between T and R) and {{c1::sequential}} (gradual transition…
Published	09/07/2023	{{c1::Allosteric}} effectors regulate the activity of a protein
Published	09/07/2023	{{c1::Heterotropic effectors}} are not “normal ligands." They bind sites distinct from the protein's active site to affect binding/activity
Published	09/07/2023	{{c1::Homotropic effectors}} are "normal" ligands that effect allosteric binding/activity
Published	09/07/2023	{{c1::2,3-BPG}} binds to Hb and stabilizes the T state favoring O2 release
Published	09/07/2023	2,3-BPG binds {{c1::HbA}} more tightly than {{c1::HbF}}. This allows O2 to be transferred from the mother to the fetus.
Published	09/07/2023	The {{c1::Bohr Effect}} describes how protons and CO2 favor the T state of Hb
Published	09/07/2023	{{c1::Protons}} stabilize salt bridges in the T state of Hb
Published	09/07/2023	Hb can physically bind {{c1::CO2}}, transporting it to the lungs (where lower {{c1::CO2}} partial pressure causes {{c1::CO2}} release)
Published	09/07/2023	What are the 3 key regulators of Hb?{{c1::2,3-BPGpHCO2}}
Published	09/07/2023	2,3 BPG, pH, and CO2 can have {{c1::additive}} effects on Hb function due to {{c2::their different binding sites}}
Published	09/07/2023	{{c1::HbS}} has a simple substitution in the beta chain of the tetramer (Glu6 to Val)
Published	09/07/2023	The HbS mutation (Glu6Val) allows the newly hydrophobic patch to {{c1::polymerize}} adjacent beta subunits, but polymerization is favored in the {{c2:…
Published	09/07/2023	How are RBCs with the sickle-cell trait different than normal RBCs? {{c1::shorter lifespanblock capillaries and cause painbuild up free radicals}}
Published	09/07/2023	The HbS mutation persists because it provides some protection against {{c1::malaria}}
Published	09/07/2023	Why is CO so deadly? {{c1::it displaces O2 from Hb and binds much more tightly (200x)}}
Published	09/07/2023	{{c1::Glucose}} reacts irreversibly with HbA to form {{c1::HbA1c}}, which can be used as a marker of blood glucose levels
Status	Last Update	Fields