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• W302142773 abstract "Publisher Summary This chapter discusses the proton hyperfine resonance assignments in Glycera dibranchiata monomer hemoglobin component IV. The low-spin, cyanide-ligated Fe 3+ form of monomer Component IV are chosen for initial studies. In this paramagnetic form, the heme iron ion acts as an intrinsic shift reagent. The result is a proton nuclear magnetic resonance (NMR) spectrum that in D 2 O is spread over ∼27 ppm at 30°C, with the most highly shifted resonances due to protons located closest to the heme iron ion. In this way, a selective view of the heme site can be obtained. The hyperfine shifted resonances are extremely sensitive to structural changes in the heme pocket, and when they are completely assigned, they are expected to be effective spectroscopic probes of heme pocket integrity in expressed proteins. The chapter presents the heme coordination structure in stereo, including the orientations of the heme/proximal histidine plane for GMH4 in comparison to sperm whale myoglobin. Being monomelic hemoglobin, GMH4 is frequently compared with myoglobin because these two proteins share very similar architectures. An important aspect of the GMH4 structure is that primary sequence results and a model built from that sequence provide evidence for an unusual heme pocket." @default.
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• W302142773 date "1994-01-01" @default.
• W302142773 modified "2023-09-27" @default.
• W302142773 title "Proton Hyperfine Resonance Assignments in Glycera Dibranchiata Monomer Hemoglobin Component IV" @default.
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• W302142773 doi "https://doi.org/10.1016/b978-0-12-194710-1.50057-6" @default.
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