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  • https://bio.libretexts.org/Workbench/Biochem_Remix_Acevedo/05%3A_Protein_Function/5.02%3A_Oxygen-Binding_Proteins_and_Allosterism
    The proximal His (coordinated to the Fe 2 + ) is pulled toward the heme, which causes the F helix to shift, causing a change in the FG corner (the sequence separating the F and G helices) at the alpha...The proximal His (coordinated to the Fe 2 + ) is pulled toward the heme, which causes the F helix to shift, causing a change in the FG corner (the sequence separating the F and G helices) at the alpha-beta interface as well as the C and G helices at the interface, which all slide past each other to the oxy-or R conformation.
  • https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/05%3A_Protein_Function/5.03%3A_B._Other_Allosteric_Proteins
    This page covers the intricacies of allosterism in biochemistry, focusing on myoglobin, hemoglobin, and various enzymes, including lactate dehydrogenase and phosphofructokinases. It discusses structur...This page covers the intricacies of allosterism in biochemistry, focusing on myoglobin, hemoglobin, and various enzymes, including lactate dehydrogenase and phosphofructokinases. It discusses structural transformations in viral enzymes and the significance of Lenacapavir as an HIV drug. The text details the kinetic behaviors of enzymes and the influence of ligand concentrations on activity.
  • https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/08%3A_Enzyme_Regulation/8.04%3A_Oxygen-Binding_Proteins_and_Allosterism

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