Structural dynamics of liganded myoglobin
نویسندگان
چکیده
منابع مشابه
Cavities and packing defects in the structural dynamics of myoglobin.
Small globular proteins contain internal cavities and packing defects that reduce thermodynamic stability but seem to play a role in controlling function by defining pathways for the diffusion of the ligand/substrate to the active site. In the case of myoglobin (Mb), a prototype for structure-function relationship studies, the photosensitivity of the adduct of the reduced protein with CO, O2 an...
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The EFG-tensor at the position of the Fe-atom of CO-liganded sperm whale myoglobin has been investigated by nuclear gamma-resonance absorption experiments on single crystals. In addition the temperature dependence of the quadrupole splitting of the 14.4 keV level of the iron nucleus was measured. An unambiguous solution for the magnitude and the orientation of the field gradient tensor could on...
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To unveil the mechanism of fast autooxidation of fish myoglobins, the effect of temperature on the structural change of tuna myoglobin was investigated. Purified myoglobin was subjected to preincubation at 5, 20, 50 and 40C. Overall helical structural decay through thermal treatment up to 95C was monitored by circular dichroism spectrometry, while the structural changes around the heme pocket w...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1980
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(80)84984-8