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.
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Ginsburg, A. Reversible, Thermally Induced Domain Unfolding in Oligomeric Proteins. Spectral and DSC measurements. Journal of Thermal Analysis and Calorimetry 61, 425–436 (2000). https://doi.org/10.1023/A:1010113300190
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DOI: https://doi.org/10.1023/A:1010113300190