Structure and stability of a rat odorant-binding protein: another brick in the wall.
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.
Scirè
Andrea
A
Department of Biochemistry, Biology, and Genetics, Universita Politecnica delle Marche, Ancona, Italy.
Marabotti
Anna
A
Staiano
Maria
M
Briand
Loic
L
Varriale
Antonio
A
Bertoli
Enrico
E
Tanfani
Fabio
F
D'Auria
Sabato
S
D000818:Animals; D003198:Computer Simulation; D016018:Least-Squares Analysis; D008958:Models, Molecular; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D051381:Rats; D018035:Receptors, Odorant / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D018035:Receptors, Odorant; D011994:Recombinant Proteins; C045648:odorant-binding protein