MM/PBSA analysis of molecular dynamics simulations of bovine beta-lactoglobulin: free energy gradients in conformational transitions? (Articolo in rivista)

Type

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

Label

• MM/PBSA analysis of molecular dynamics simulations of bovine beta-lactoglobulin: free energy gradients in conformational transitions? (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1002/prot.20384 (literal)

Alternative label

• Fogolari F.; Moroni E.; Wojciechowski M.; Baginski M.; Ragona L.; Molinari H. (2005)
  MM/PBSA analysis of molecular dynamics simulations of bovine beta-lactoglobulin: free energy gradients in conformational transitions?
  in Proteins (Print)
  (literal)

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

• Fogolari F.; Moroni E.; Wojciechowski M.; Baginski M.; Ragona L.; Molinari H. (literal)

Pagina inizio

• 91 (literal)

Pagina fine

• 103 (literal)

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

• 59 (literal)

Rivista

• Proteins (Rivista)

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

• 1 (literal)

Note

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

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

• Ragona L, ISMAC-CNR Fogolari F, Molinari H.: Uni. Verona Moroni E, Uni. Milano Bicocca Wojciechowski M, Baginski M, Uni. Gdansk, Polonia (literal)

Titolo

• MM/PBSA analysis of molecular dynamics simulations of bovine beta-lactoglobulin: free energy gradients in conformational transitions? (literal)

Abstract

• The pH-driven opening and closure of beta-lactoglobulin ET loop, acting as a lid and closing the internal cavity of the protein, has been studied by molecular dynamics (MD) simulations and free energy calculations based on molecular mechanics/Poisson-Boltzmann (PB) solvent-accessible surface area (MM/PBSA) methodology. The forms above and below the transition pH differ presumably only in the protonation state of residue Glu89. MM/PBSA calculations are able to reproduce qualitatively the thermodynamics of the transition. The analysis of MD simulations using a combination of MM/PBSA methodology and the colony energy approach is able to highlight the driving forces implied in the transition. The analysis suggests that global rearrangements take place before the equilibrium local conformation is reached. This conclusion may bear general relevance to conformational transitions in all lipocalins and proteins in general. (literal)

Prodotto di

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

Autore CNR

• LAURA GIUDITTA RAGONA (Unità di personale interno)

Insieme di parole chiave

• Keywords of "MM/PBSA analysis of molecular dynamics simulations of bovine beta-lactoglobulin: free energy gradients in conformational transitions?" (Insieme di parole chiave)

Incoming links:

Prodotto

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

Autore CNR di

• LAURA GIUDITTA RAGONA (Unità di personale interno)

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

• Proteins (Rivista)

Insieme di parole chiave di

• Keywords of "MM/PBSA analysis of molecular dynamics simulations of bovine beta-lactoglobulin: free energy gradients in conformational transitions?" (Insieme di parole chiave)