title: [Effect of temperature on intramolecular dynamics and conformational state of bacterial alkaline phosphatase].
abstract: The slow internal dynamics and the conformational state of Escherichia coli alkaline phosphatase by the action of temperature in the range 0-100 degrees C have been investigated by tryptophan room temperature phosphorescence and fluorescence. It has been shown that heating an alkaline phosphatase solution in the interval 0-70 degrees C leads to a substantial increase in the slow internal dynamics. A further increase in temperature to 95 degrees C causes a reversible enhancement of internal dynamics and a partial unfolding of the globule. Heating the protein solution in a narrow temperature range 97-100 degrees C induces an irreversible conformational transition, which is characterized by total unfolding of the globule, a drastic increase in internal dynamics, and the loss of enzymatic activity.
authors.forename: V M
authors.initials: VM
authors.lastname: Mazhul'
authors.forename: S Zh
authors.initials: SZh
authors.lastname: Kananovich
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D006361:Heating; D011487:Protein Conformation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D000469:Alkaline Phosphatase