Abstract
Room-temperature tryptophan phosphorescence and fluorescence have been used to study the slow internal dynamics and the conformational state of Escherichia coli alkaline phosphatase in the temperature range from 0 to 100°C. The heating of alkaline phosphatase solution within the 0–70°C range has been shown to amplify considerably the internal dynamics. The further raise of temperature to 95°C brings about a reversible increase in the internal dynamics and partial unfolding of the globule. The heating of protein solution within a narrow temperature range of 97–100°C gives rise to irreversible conformational transition with complete globule unfolding, sharp amplification of the internal dynamics, and loss of enzymatic activity.
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