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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of thermal analysis and calorimetry 61 (2000), S. 425-436 
    ISSN: 1572-8943
    Keywords: Acanthamoeba myosin II rod coiled-coil ; amino terminal domain of enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system of E. coli ; circular dichroism ; differential scanning calorimetry ; dodecameric glutamine synthetase ; oligomeric protein domains ; thermal unfolding ; UV-spectra
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Spectral and differential scanning calorimetry (DSC) results for three oligomeric proteins are briefly reviewed. (A) Reversible, thermally-induced partial unfolding reactions in dodecameric glutamine synthetase from E. coli involve cooperative, two two-state transitions of subunits and demonstrate communication among subunits. (B) Thermal unfolding of intact Acanthamoeba myosin II is more cooperative than that of mammalian skeletal muscle myosin. Nucleotide-induced conformational changes thermally stabilize head domains in both myosins. The long dimeric coiled-coil rod of Acanthamoeba myosin II undergoes a reversible, cooperative, single two-state thermal transition with concomitant chain dissociation. (C) The amino terminal domain of enzyme I of the E. coliPEP:sugar phosphotransferase system is destabilized by phosphorylation of the active-site His 189.
    Type of Medium: Electronic Resource
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