Pyramidalization of backbone carbonyl carbon atoms in proteins. (Articolo in rivista)

Type

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

Label

• Pyramidalization of backbone carbonyl carbon atoms in proteins. (Articolo in rivista) (literal)

Anno

• 2000-01-01T00:00:00+01:00 (literal)

Alternative label

• Esposito, L., Vitagliano, L., Zagari, A., Mazzarella, L. (2000)
  Pyramidalization of backbone carbonyl carbon atoms in proteins.
  in Protein science (Print)
  (literal)

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

• Esposito, L., Vitagliano, L., Zagari, A., Mazzarella, L. (literal)

Pagina inizio

• 2038 (literal)

Pagina fine

• 2042 (literal)

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

• 9 (literal)

Rivista

• Protein science (Rivista)

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

• Centro di Studio di Biocristallografia, CNR, Via Mezzocannone 4, I-80134 Napoli, Italy Dipartimento di Chimica, Università degli Studi di Napoli \"Federico II\", Via Mezzocannone 4, I-80134 Napoli, Italy (literal)

Titolo

• Pyramidalization of backbone carbonyl carbon atoms in proteins. (literal)

Abstract

• The high accuracy of X-ray analyses at atomic resolution is now able to display subtle deformations from standard geometry of building blocks in proteins. From the analysis of nine ultra-high resolution protein structures, we derived the first experimental evidence that a significant pyramidalization at the mainchain carbonyl carbon atom occurs in proteins. Our findings also show that this pyramidalization is related to the main-chain psi torsion angle. The carbonyl carbon atoms of residues that adopt alphaR and extended conformations show a clear preference for positive and negative pyramidalization, respectively. The agreement between our data and those previously obtained from small molecule structures demonstrates that carbon pyramidalization is an intrinsic property of the peptide structure. Although small in magnitude, the pyramidalization is well preserved in the complex folded state of a macromolecular structure that results from the interplay of many different forces. In addition, this property of the peptide group may have interesting implications for the enzymatic reactions involving the carbonyl carbon atoms. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• LUCIANA ESPOSITO (Unità di personale interno)
• LUIGI VITAGLIANO (Persona)

Incoming links:

Autore CNR di

• LUIGI VITAGLIANO (Persona)
• LUCIANA ESPOSITO (Unità di personale interno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)

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

• Protein science (Rivista)