Registro completo |
Provedor de dados: |
Inra
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País: |
France
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Título: |
Structure and stability of a rat odorant-binding protein: another brick in the wall
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Autores: |
Scire, A.
Marabotti, A.
Staiano, M.
Briand, L.
Varriale, A.
Bertoli, E.
Tanfani, F.
D’Auria, S.
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Data: |
2009
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Ano: |
2009
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Palavras-chave: |
ODORANT-BINDING PROTEIN
FOURIER TRANSFORM INFRARED SPECTROSCOPIE
LIPOCALIN
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Resumo: |
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.
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Tipo: |
Journal Article
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Idioma: |
Inglês
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Identificador: |
http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010bef21c07&uri=/notices/prodinra1/2010/07/
http://www.prodinra.inra.fr/prodinra/pinra/data/2010/06/PROD2010bef21c07_20100604032236772.pdf
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Formato: |
application/pdf
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Fonte: |
Journal of Proteome Research. 2009, 8 (8) : 4005-4013
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