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
URL:
http://dx.doi.org/10.1023/A:1010113300190
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