Physical and chemical perturbations induce the formation of protein aggregates with different structural features.
Protein Expr Purif
; 58(2): 356-61, 2008 Apr.
Article
em En
| MEDLINE
| ID: mdl-18226922
ABSTRACT
The in vitro aggregation of the model GST-GFP fusion protein was induced by several effectors, including those mimicking variations occurring under cell stress conditions. In particular, we examined the effects of thermal treatments, redox state and pH variations, salt addition, and freezing and thawing cycles. The resulting aggregates displayed different morphologies as seen by electron microscopy, and different secondary and tertiary structures, as indicated by Fourier transform infrared spectroscopy and fluorescence. Therefore, proteins can be forced to undergo multiple aggregation pathways that lead to assemblies with different molecular structures and, possibly, specific physiological and pathological roles. In conclusion, great caution should be taken in inferring conclusions on protein aggregation and disaggregation in vivo from results obtained using aggregates produced under non-physiological perturbations.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Recombinantes de Fusão
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Estrutura Quaternária de Proteína
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Proteínas de Fluorescência Verde
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Glutationa Transferase
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article