title: [The heat denaturation of bacterial ribonuclease studied by infrared spectroscopy].
abstract: The thermal denaturation of bacterial ribonuclease in the interval of pH 2.5-7.0 has been investigated by means of infra-red spectroscopy method. The protein melting for pH 2.5 begins at the temperature 25 degrees C and is accompanied by secondary protein structure reconstruction, partially destroying native beta-structure and leading to new denatured conformation appearance of different types of beta-turns. Spectral changes for pH 3.5 and 7.0 are significantly less in the same frequency areas. At the temperature more than 50 degrees C protein aggregation takes place with inter-molecule-beta-form formation.
authors.forename: E A
authors.initials: EA
authors.lastname: Strupishina
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D004722:Endoribonucleases / Q000032:analysis*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D011489:Protein Denaturation; D013055:Spectrophotometry, Infrared / Q000379:methods; D013696:Temperature
chemical_list: D004722:Endoribonucleases; C022543:ribonuclease T(2)
vernacular_title: Issledovanie teplovoĭ denaturatsii bakterial'noĭ ribonukleazy metodom infrakrasnoĭ spektroskopii.