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Journal

2014 | 1 | 1 |

Article title

Conformational disorder in phosphopeptides: solution studies by CD and NMR techniques

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EN

Abstracts

EN
In the last few years intrinsically disordered proteins (IDPs) have received great attention from the scientific community as they participate in several important biological processes and diseases. The intrinsic disorder and flexibility of IDPs grant them a number of advantages with respect to ordered proteins, such as conformational plasticity to bind several targets, a large interaction surface, involvement in high specificity/low affinity interactions, enhanced binding kinetics. It is assumed that post-translational modifications such as phosphorylation can stimulate structural rearrangement in IDPs and facilitate their binding to partners. To better understand at a structural level the multifaceted mechanisms that govern molecular recognition processes involving IDPs, we designed, synthesized by solid phase methods, and structurally characterized unstructured peptides. These molecules contain a putative disordered module, flanked at either the N- or C-terminal ends by a different phosphorylated amino acid (serine or threonine) to mimick the effects of phosphorylation. The absence of an ordered state in the designed peptides was proved experimentally by CD and NMR conformational studies that were carried out under different solution conditions

Publisher

Journal

Year

Volume

1

Issue

1

Physical description

Dates

published
1 - 1 - 2014
online
2 - 7 - 2014

Contributors

  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy
  • University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
  • Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
author
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
  • CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse - UMR 7282, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy/ Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.-psjd-doi-10_2478_ped-2014-0001
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