Peptide bond distortions from planarity: new insights from quantum mechanical calculations and peptide/protein crystalstructures (Articolo in rivista)

Type

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

Label

• Peptide bond distortions from planarity: new insights from quantum mechanical calculations and peptide/protein crystalstructures (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

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

• 10.1371/journal.pone.0024533 (literal)

Alternative label

• Improta R, Vitagliano L, Esposito L. (2011)
  Peptide bond distortions from planarity: new insights from quantum mechanical calculations and peptide/protein crystalstructures
  in PloS one
  (literal)

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

• Improta R, Vitagliano L, Esposito L. (literal)

Pagina inizio

• e24533 (literal)

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

• 6 (literal)

Rivista

• PloS one (Rivista)

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

• 9 (literal)

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

• Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Napoli, Italy (literal)

Titolo

• Peptide bond distortions from planarity: new insights from quantum mechanical calculations and peptide/protein crystalstructures (literal)

Abstract

• By combining quantum-mechanical analysis and statistical survey of peptide/protein structure databases we here report a thorough investigation of the conformational dependence of the geometry of peptide bond, the basic element of protein structures. Different peptide model systems have been studied by an integrated quantum mechanical approach, employing DFT, MP2 and CCSD(T) calculations, both in aqueous solution and in the gas phase. Also in absence of inter-residue interactions, small distortions from the planarity are more a rule than an exception, and they are mainly determined by the backbone ? dihedral angle. These indications are fully corroborated by a statistical survey of accurate protein/peptide structures. Orbital analysis shows that orbital interactions between the ? system of C(?) substituents and the ? system of the amide bond are crucial for the modulation of peptide bond distortions. Our study thus indicates that, although long-range inter-molecular interactions can obviously affect the peptide planarity, their influence is statistically averaged. Therefore, the variability of peptide bond geometry in proteins is remarkably reproduced by extremely simplified systems since local factors are the main driving force of these observed trends. The implications of the present findings for protein structure determination, validation and prediction are also discussed. (literal)

Prodotto di

• Le proprietà magnetiche di radicali di interesse biologico ed ambientale: un approccio multiscala (PM.P07.005.003) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• ROBERTO IMPROTA (Persona)
• LUCIANA ESPOSITO (Persona)
• LUIGI VITAGLIANO (Persona)

Incoming links:

Autore CNR di

• LUIGI VITAGLIANO (Persona)
• ROBERTO IMPROTA (Persona)
• LUCIANA ESPOSITO (Persona)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Le proprietà magnetiche di radicali di interesse biologico ed ambientale: un approccio multiscala (PM.P07.005.003) (Modulo)

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

• PloS one (Rivista)