http://www.cnr.it/ontology/cnr/individuo/prodotto/ID168583

Structure and stability of a rat odorant-binding protein. Another brick in the wall (Articolo in rivista)

Type

Label

Structure and stability of a rat odorant-binding protein. Another brick in the wall (Articolo in rivista) (literal)

Anno

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Alternative label

Scirè A.; Marabotti A.; Staiano M.; Briand L.; Varriale A.; Bertoli E.; Tanfani F.; D'Auria S. (2009)
Structure and stability of a rat odorant-binding protein. Another brick in the wall
in Journal of proteome research (Print); ACS, American chemical society, Washington, DC (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Scirè A.; Marabotti A.; Staiano M.; Briand L.; Varriale A.; Bertoli E.; Tanfani F.; D'Auria S. (literal)

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Note

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Department of Biochemistry, Biology, and Genetics, Universita? Politecnica delle Marche, Ancona, Italy, Institute of Food Sciences, CNR, Avellino, Italy, Laboratory for Molecular Sensing, IBP, CNR, Naples, Italy, and UMR FLAVIC INRA-ENESAD - University of Bourgogne, 17 rue Sully, BP 86510 21065 Dijon, Cedex, France (literal)

Titolo

Structure and stability of a rat odorant-binding protein. Another brick in the wall (literal)

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. (literal)

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