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Structure and Stability of a Rat Odorant-Binding Protein: Another Brick in the Wall

2009; American Chemical Society; Volume: 8; Issue: 8 Linguagem: Inglês

10.1021/pr900346z

1535-3907

Andrea Scirè, Anna Marabotti, Maria Staiano, Loı̈c Briand, Antonio Varriale, Enrico Bertoli, Fabio Tanfani, Sabato D’Auria,

Lipid Membrane Structure and Behavior

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.