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- W1965875500 abstract "Hemoglobin has been a long-standing paradigm for understanding protein allostery. Here, the x-ray structures of two chemically crosslinked, fully liganded hemoglobins, α 2 β 82 CA 82 β and α 2 β 82 ND 82 β, are described at 2.3 Å and 2.6 Å resolution, respectively. Strikingly, these crosslinked hemoglobins assume intermediate conformations that lie between those of R and the controversial liganded hemoglobin state R2 rather than between R and T. Thus, these structures support only a T ↔ R ↔ R2 allosteric pathway and underscore the physiological importance of the R2 conformation." @default.
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- W1965875500 date "1997-07-22" @default.
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- W1965875500 title "Allosteric intermediates indicate R2 is the liganded hemoglobin end state" @default.
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- W1965875500 doi "https://doi.org/10.1073/pnas.94.15.7841" @default.
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