Abstract
The effect of temperature on the structure of the rat odorant-binding protein was investigated by spectroscopic and in silico methodologies. In particular, in this work, we examined the structural features of the rat OBP-1F by Fourier-transform infrared spectroscopy and molecular dynamics investigations. The obtained spectroscopic results were analyzed using the following three different methods based on the unexchanged amide hydrogens of the protein sample: (1) the analysis of difference spectra; (2) the generalized 2D-IR correlation spectroscopy; (3) the phase diagram method. The three methods indicated that at high temperatures the rOBP-1F structure undergoes a relaxation process involving the protein tertiary organization before undergoing the denaturation and aggregation processes, suggesting the presence of an intermediate state such as a molten globule-like state. Importantly, the proposed analyses represent a general approach that could be applied to the study of protein stability.
Original language | English |
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Pages (from-to) | 4005-4013 |
Number of pages | 9 |
Journal | Journal of Proteome Research |
Volume | 8 |
Issue number | 8 |
DOIs | |
Publication status | Published - Aug 7 2009 |
Keywords
- Fourier transform infrared spectroscopy
- Lipocalin
- Odorant-binding protein
ASJC Scopus subject areas
- Biochemistry
- Chemistry(all)