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NMR studies of BPTI aggregation by using paramagnetic relaxation reagents

  • Andrea Bernini
  • , Ottavia Spiga
  • , Arianna Ciutti
  • , Vincenzo Venditti
  • , Filippo Prischi
  • , Mariangela Governatori
  • , Luisa Bracci
  • , Barbara Lelli
  • , Silvia Pileri
  • , Mauro Botta
  • , Alessandro Barge
  • , Franco Laschi
  • , Neri Niccolai

Research output: Contribution to journalArticlepeer-review

Abstract

Paramagnetic probes, whose approach to proteins can be monitored by nuclear magnetic resonance (NMR) studies, have been found of primary relevance for investigating protein surfaces accessibility. Here, paramagnetic probes are also suggested for a systematic investigation on protein aggregation. Bovin pancreatic trypsin inhibitor (BPTI) was used as a model system for aggregation by analyzing its interaction with TEMPOL and Gd(III)DTPA-BMA. Some of the measured paramagnetic relaxation rates of BPTI protons exhibited a reverse dependence on protein concentration, which can be attributed to the formation of transient BPTI aggregates.

Original languageEnglish
Pages (from-to)856-862
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1764
Issue number5
DOIs
Publication statusPublished - May 2006

Keywords

  • BPTI
  • Gd(III)DTPA-BMA
  • NMR
  • Paramagnetic probe
  • Protein aggregation
  • Surface accessibility
  • TEMPOL

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