Molecular Spacers for Physicochemical Investigations Based on Novel Helical and Extended Peptide Structures (Articolo in rivista)

Type

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

Label

• Molecular Spacers for Physicochemical Investigations Based on Novel Helical and Extended Peptide Structures (Articolo in rivista) (literal)

Anno

• 2004-01-01T00:00:00+01:00 (literal)

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

• 10.1002/bip.10575 (literal)

Alternative label

• Toniolo C., Crisma M., Formaggio F., Peggion C., Broxterman Q.B., Kaptein B. (2004)
  Molecular Spacers for Physicochemical Investigations Based on Novel Helical and Extended Peptide Structures
  in Biopolymers (Print)
  (literal)

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

• Toniolo C., Crisma M., Formaggio F., Peggion C., Broxterman Q.B., Kaptein B. (literal)

Pagina inizio

• 162 (literal)

Pagina fine

• 176 (literal)

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

• Citazioni WOS: 43 Impact Factor 2004: 2.863 Coautore (literal)

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

• 76 (literal)

Rivista

• Biopolymers (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy; DSM Research, Pharma-Chemicals, Advanced Synthesis and Catalysis, 6160 MD Geleen, The Netherlands (literal)

Titolo

• Molecular Spacers for Physicochemical Investigations Based on Novel Helical and Extended Peptide Structures (literal)

Abstract

• A proper understanding of the detailed nature and mechanism of physicochemical interactions depends heavily upon our ability to design and synthesize conformationally constrained 3D structures whose intercomponent geometry (either rigorously, rigid or able to undergo destructuration, if required, but in all cases precisely tunable) would be well defined. To this end we have recently reported a few initial studies and we are currently working on the exploitation of stable, short, helical peptide spacers based on achiral ond/or chiral Calpha-tetrasubstituted alpha-amino acids. These building blocks are known to force the peptides either to predominantly fold into a 3(10)-helical structure or to adopt a fully extended, planar 2.0(5)-helix. The systems under investigation involve a donor and an acceptor moiety linked to the N- and C-termini of the oligopeptide spacer main chain. By increasing the number of intervening residues the donor(...)acceptor separation can be easily, modulated. This review highlights details of these two novel peptide secondary structures and their use as molecular spacers in physicochemical investigations. (literal)

Prodotto di

• Institute of biomolecular chemistry (ICB) (Istituto)

Autore CNR

• MARCO CRISMA (Unità di personale interno)

Incoming links:

Autore CNR di

• MARCO CRISMA (Unità di personale interno)

Prodotto

• Institute of biomolecular chemistry (ICB) (Istituto)

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

• Biopolymers (Rivista)