BSC 450 Lecture Notes - Lecture 10: Citric Acid Cycle, Peptide, Mutation

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Hemoglobin has a heterotetrameric structure: hemoglobin (hb) is a tetramer of two subunits ( 2 2, each subunit is similar to myoglobin. How can affinity to oxygen change: must be a protein with multiple binding sites, binding sites must be able to interact with each other. Hb hbo2 hb(o2)2 hb(o2)3 hb(o2)4. R and t states of hemoglobin: t = tense/tight state, more interactions, more stable, tissues, r = relaxed state, fewer interactions, more flexible, higher affinity for o2, lungs, o2 binding triggers a t --. R conformational change: conformational change from the t state to the r state involves breaking ion pairs between the 1- 2 interface. 2,3-bisphosphoglycerate regulates o2 binding: negative heterotropic regulator of hb function, small negatively charged molecule, binds to the positively charged central cavity of hb, stabilizes the t state, fits into central cavity of the t state.

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