Site-specific investigation of the steady-state kinetics and dynamics of the multistep binding of bile Acid molecules to a lipid carrier protein (Articolo in rivista)

Type

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

Label

• Site-specific investigation of the steady-state kinetics and dynamics of the multistep binding of bile Acid molecules to a lipid carrier protein (Articolo in rivista) (literal)

Anno

• 2010-01-01T00:00:00+01:00 (literal)

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

• 10.1002/chem.201000498 (literal)

Alternative label

• Cogliati C; Ragona L; D'Onofrio M; Günther U; Whittaker S; Ludwig C; Tomaselli S; Assfalg M; Molinari H (2010)
  Site-specific investigation of the steady-state kinetics and dynamics of the multistep binding of bile Acid molecules to a lipid carrier protein
  in Chemistry (Weinh., Print)
  (literal)

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

• Cogliati C; Ragona L; D'Onofrio M; Günther U; Whittaker S; Ludwig C; Tomaselli S; Assfalg M; Molinari H (literal)

Pagina inizio

• 11300 (literal)

Pagina fine

• 11310 (literal)

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

• http://www.chemeurj.org (literal)

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

• 16 (literal)

Rivista

• Chemistry (Rivista)

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

• 37 (literal)

Note

• Scopu (literal)
• ISI Web of Science (WOS) (literal)

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

• Cogliati C. - Ismac-Milano, Ragona L. - Ismac-Milano, D'Onofrio M- Università di Verona Gunther U- University of Birmingham, UK Whittaker S, University of Birmingham, UK Ludwig C, University of Birmingham, UK Tomaselli S. - Ismac-Milano Assfalg M - Università di Verona Molinari H- Università di Verona (literal)

Titolo

• Site-specific investigation of the steady-state kinetics and dynamics of the multistep binding of bile Acid molecules to a lipid carrier protein (literal)

Abstract

• The investigation of multisite ligand-protein binding and multistep mechanisms is highly demanding. In this work, advanced NMR methodologies such as 2D 1H-15N line-shape analysis, which allows a reliable investigation of ligand binding occurring on micro- to millisecond timescales, have been extended to model a two-step binding mechanism. The molecular recognition and complex uptake mechanism of two bile salt molecules by lipid carriers is an interesting example that shows that protein dynamics has the potential to modulate the macromolecule- ligand encounter. Kinetic analysis supports a conformational selection model as the initial recognition process in which the dynamics observed in the apo form is essential for ligand uptake, leading to conformations with improved access to the binding cavity. Subsequent multi-step events could be modelled, for several residues, with a two-step binding mechanism. The protein in the ligand-bound state still exhibits a conformational rearrangement that occurs on a very slow timescale, as observed for other proteins of the family. A global mechanism suggesting how bile acids access the macromolecular cavity is thus proposed. (literal)

Prodotto di

• Strutturistica NMR di proteine legate a processi patologici (PM.P01.026.003) (Modulo)
• Istituto per lo studio delle macromolecole (ISMAC) (Istituto)

Autore CNR

• SIMONA TOMASELLI (Unità di personale interno)
• LAURA GIUDITTA RAGONA (Unità di personale interno)
• CLELIA COGLIATI (Unità di personale esterno)

Insieme di parole chiave

• Keywords of "Site-specific investigation of the steady-state kinetics and dynamics of the multistep binding of bile Acid molecules to a lipid carrier protein" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• SIMONA TOMASELLI (Unità di personale interno)
• LAURA GIUDITTA RAGONA (Unità di personale interno)
• CLELIA COGLIATI (Unità di personale esterno)

Prodotto

• Istituto per lo studio delle macromolecole (ISMAC) (Istituto)
• Strutturistica NMR di proteine legate a processi patologici (PM.P01.026.003) (Modulo)

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

• Chemistry (Rivista)

Insieme di parole chiave di

• Keywords of "Site-specific investigation of the steady-state kinetics and dynamics of the multistep binding of bile Acid molecules to a lipid carrier protein" (Insieme di parole chiave)