A role for molecular compression in the post-translational formation of the Green Fluorescent Protein chromophore (Articolo in rivista)

Type

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

Label

• A role for molecular compression in the post-translational formation of the Green Fluorescent Protein chromophore (Articolo in rivista) (literal)

Anno

• 2010-01-01T00:00:00+01:00 (literal)

Alternative label

• Terranova U. and Nifosi R. (2010)
  A role for molecular compression in the post-translational formation of the Green Fluorescent Protein chromophore
  in Chemical physics (Print)
  (literal)

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

• Terranova U. and Nifosi R. (literal)

Pagina inizio

• 76 (literal)

Pagina fine

• 83 (literal)

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• 371 (literal)

Rivista

• Chemical physics (Rivista)

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• Acknowledgement: The authors gratefully acknowledge support from CNR-INFM through \"Iniziativa Calcolo Parallelo\" at the CINECA Supercomputing Center, Bologna, Italy. (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• 1. CNR, NEST, I-56126 Pisa, Italy (Nifosi R.) 2. Scuola Normale Super Pisa, I-56126 Pisa, Italy (Nifosi R.) 3. UCL, Dept Phys & Astron, London WC1E 6BT, England (Terranova U.) 4. London Ctr Nanotechnol, London WC1H 0AH, England (Terranova U.) (literal)

Titolo

• A role for molecular compression in the post-translational formation of the Green Fluorescent Protein chromophore (literal)

Abstract

• Spontaneous chromophore formation is probably the key feature for the remarkable success of GFPs (Green Fluorescent Proteins) and related proteins in fluorescence microscopy. Though a quantitative analysis of the involved energetics still remains elusive, substantial progress has been made in identifying the steps of chromophore biosynthesis and the contribution of individual residues and surrounding protein matrix. The latter clearly enforces a peculiar configuration of the pre-cyclized chromophore-forming tripeptide. However, it is debated whether a mechanical compression is also at play in triggering backbone cyclization. Here, by molecular dynamics and potential of mean force calculations, we estimate the contribution of the protein scaffold in promoting the proximity of reacting atoms-and hence backbone cyclization - by a sort of compression mechanism. Comparing several mutants we highlight the role of some surrounding residues. Finally, we analyze the case of HAL (Histidine Ammonia-Lyase) active site, which undergoes an analogous cyclization reaction. (C) 2010 Elsevier B.V. All rights reserved. (literal)

Prodotto di

• Progettazione ed applicazioni di Nanobiotecnologie (MD.P06.022.002) (Modulo)

Autore CNR

• RICCARDO NIFOSI' (Persona)

Insieme di parole chiave

• Parole chiave di "A role for molecular compression in the post-translational formation of the Green Fluorescent Protein chromophore" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• RICCARDO NIFOSI' (Persona)

Prodotto

• Progettazione ed applicazioni di Nanobiotecnologie (MD.P06.022.002) (Modulo)

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

• Chemical physics (Rivista)

Insieme di parole chiave di

• Parole chiave di "A role for molecular compression in the post-translational formation of the Green Fluorescent Protein chromophore" (Insieme di parole chiave)