Insight into Ribonuclease A Domain Swapping by Molecular Dynamics Unfolding Simulations (Articolo in rivista)

Type

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

Label

• Insight into Ribonuclease A Domain Swapping by Molecular Dynamics Unfolding Simulations (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1021/bi0488350 (literal)

Alternative label

• Esposito, Luciana; Daggett, Valerie (2005)
  Insight into Ribonuclease A Domain Swapping by Molecular Dynamics Unfolding Simulations
  in Biochemistry (Easton)
  (literal)

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

• Esposito, Luciana; Daggett, Valerie (literal)

Pagina inizio

• 3358 (literal)

Pagina fine

• 3368 (literal)

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

• 44 (literal)

Rivista

• Biochemistry (Rivista)

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

• Pubblicazione su rivista internazionale (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy, and Department of Medicinal Chemistry, UniVersity of Washington, Seattle, Washington 98195-7610 (literal)

Titolo

• Insight into Ribonuclease A Domain Swapping by Molecular Dynamics Unfolding Simulations (literal)

Abstract

• Bovine pancreatic RNase (RNase A) deserves a special place among the numerous proteins that form oligomers by three-dimensional domain swapping. In fact, under destabilizing conditions and at high protein concns., it can swap two different domains, the N-terminal a-helix or the C-terminal b-strand, leading to dimers with different quaternary structures. With the change in the unfolding conditions, the relative abundance of the two dimers varies, and the prevalence of one dimer over the other is inverted. To investigate the dynamic behavior of the termini, four independent 10 ns high-temp. mol. dynamics simulations of RNase A were carried out at two different pH values in an attempt to reproduce the exptl. conditions of neutral and very low pH that favor the formation of the N- and C-terminal domain-swapped dimers, resp. In agreement with exptl. data, under mild unfolding conditions, a partial or complete opening of the N-terminal arm is obsd., whereas the dislocation of the C-terminus away from the core of the structure occurs only during the low-pH simulations. Furthermore, the picture emerging from this study indicates that the same protein can have different pathways for domain swapping. Indeed, in RNase A the C-terminal swapping requires a substantial unfolding of the monomers, whereas the N-terminal swapping can occur through only partial unfolding. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Modelli molecolari per lo studio di malattie conformazionali (PM.P01.004.003) (Modulo)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR

• LUCIANA ESPOSITO (Persona)

Insieme di parole chiave

• Keywords of "Insight into Ribonuclease A Domain Swapping by Molecular Dynamics Unfolding Simulations" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• LUCIANA ESPOSITO (Persona)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)
• Modelli molecolari per lo studio di malattie conformazionali (PM.P01.004.003) (Modulo)

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

• Biochemistry (Rivista)

Insieme di parole chiave di

• Keywords of "Insight into Ribonuclease A Domain Swapping by Molecular Dynamics Unfolding Simulations" (Insieme di parole chiave)