A Simple Mechanism Underlying the Effect of Protecting Osmolytes on Protein Folding (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• A Simple Mechanism Underlying the Effect of Protecting Osmolytes on Protein Folding (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

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

• 10.1021/ct200471w (literal)

Alternative label

• Saladino, G.; Marenchino, M.; Pieraccini, S.; Campos-Olivas, R.; Sironi, M.; Gervasio, F. L. (2011)
  A Simple Mechanism Underlying the Effect of Protecting Osmolytes on Protein Folding
  in Journal of chemical theory and computation; American Chemical Society, Washington, DC (Stati Uniti d'America)
  (literal)

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

• Saladino, G.; Marenchino, M.; Pieraccini, S.; Campos-Olivas, R.; Sironi, M.; Gervasio, F. L. (literal)

Pagina inizio

• 3846 (literal)

Pagina fine

• 3852 (literal)

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

• 7 (literal)

Rivista

• Journal of chemical theory and computation (Rivista)

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

• 7 (literal)

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

• 11 (literal)

Note

• ISI Web of Science (WoS) (literal)

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

• University of Milan; Spanish National Cancer Research Centre; INSTM Res Unit; Inst Mol Sci & Technol (literal)

Titolo

• A Simple Mechanism Underlying the Effect of Protecting Osmolytes on Protein Folding (literal)

Abstract

• Osmolytes are small organic compounds that confer to the cell an enhanced adaptability to external conditions. Many osmolytes not only protect the cell from osmotic stress but also stabilize the native structure of proteins. While simplified models able to predict changes to protein stability are available, a general physicochemical explanation of the underlying microscopic mechanism is still missing. Here, we address this issue by performing very long all-atom MD simulations, free energy calculations, and experiments on a well-characterized mini-protein, the villin headpiece. Comparisons between the folding free energy landscapes in pure water and osmolyte solutions, together with experimental validation by means of circular dichroism, unfolding experiments, and NMR, led us to formulate a simple hypothesis for the protecting mechanism. Taken together, our results support a novel mechanistic explanation according to which the main driving force behind native state protection is a change in the solvent rotational diffusion. (literal)

Editore

• American Chemical Society (Editore)

Prodotto di

• Nanoingegneria chimica di sistemi assemblati mediante interazioni intermolecolari specifiche (PM.P07.002.002) (Modulo)
• Istituto di scienze e tecnologie molecolari (ISTM) (Istituto)

Autore CNR

• Stefano Pieraccini (Persona)
• Maurizio Sironi (Persona)

Incoming links:

Prodotto

• Istituto di scienze e tecnologie molecolari (ISTM) (Istituto)
• Nanoingegneria chimica di sistemi assemblati mediante interazioni intermolecolari specifiche (PM.P07.002.002) (Modulo)

Autore CNR di

• Stefano Pieraccini (Persona)
• Maurizio Sironi (Persona)

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

• Journal of chemical theory and computation (Rivista)

Editore di

• American Chemical Society (Editore)