[Nonmonotonous character of temperature changes in protein conformation in predenaturational regions of temperatures].
Temperature changes of protein infrared spectra have a nonmonotonous pattern. On the curves of temperature relationships of spectral characteristics the regions of high frequency displacement have been observed, interrupted by sharp low frequency shifts, partly or entirely compensating the displacement of the bands in the preceding temperature interval. It has been shown that at temperatures corresponding to the high frequency displacement heat weakening of the strength of hydrogen bonds takes place. At the low frequency shifts the whole system of the hydrogen bonds has an opposite change of the state maintaining high stability level of protein macromolecules in the broad temperature range.
D006860:Hydrogen Bonding; D011487:Protein Conformation; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine; D013055:Spectrophotometry, Infrared; D013696:Temperature; D014357:Trypsin
D012710:Serum Albumin, Bovine; D014357:Trypsin
Nemonotonnyĭ kharakter temperaturnykh izmeneniĭ konformatsii belkov v preddenaturatsionnoĭ oblasti temperatur.