NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz

Ivano Bertini, Yogesh K. Gupta, Claudio Luchinat, Giacomo Parigi, Christian Schlörb, Harald Schwalbe

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

(Graph Presented) Relaxation time: Direct profiles of protein 1H relaxation in D2O at mM concentrations were generated by NMR spectroscopy at 0.01-50 MHz (see picture). The study of lysozyme at pH 3.5 (monomeric) and pH 9.0 (dimeric), and of α-synuclein (unfolded), provides direct information on aggregation through estimates of the realignment correlation time and on the overall compactness of the protein.

Original languageEnglish (US)
Pages (from-to)2223-2225
Number of pages3
JournalAngewandte Chemie - International Edition
Volume44
Issue number15
DOIs
StatePublished - Apr 8 2005
Externally publishedYes

Keywords

  • Aggregation
  • Deuterium
  • Protein folding
  • Protein structures
  • Protonation

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Fingerprint Dive into the research topics of 'NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz'. Together they form a unique fingerprint.

Cite this