title: [Thermostability of protein structure in the native state and mechanisms of its maintenance].
abstract: A comparison of temperature changes of the protein spectra with temperature behavior of other systems with hydrogen bonds shows high thermostability of the functional active structure of protein molecules. The stability of proteins space organization is regulated and supported by non-monotonous temperature changes of this organization. The physical mechanism of thermostabilization includes interaction of hydrophobic radicals of protein with the aqueous environment.
authors: A P
authors: AP
authors: Zhukovskiĭ
authors: A I
authors: AI
authors: Khaloimov
authors: N V
authors: NV
authors: Rovnov
authors: A N
authors: AN
authors: Raev
mesh_terms: D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008954:Models, Biological; D011487:Protein Conformation; D011489:Protein Denaturation; D013053:Spectrophotometry
vernacular_title: Termostabil'nost' struktury belkov v nativnom sostoianii i mekhanism ee podderzhaniia.