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Wiley, Angewandte Chemie, 15(117), p. 2263-2265, 2005

DOI: 10.1002/ange.200462344

Wiley, Angewandte Chemie International Edition, 15(44), p. 2223-2225, 2005

DOI: 10.1002/anie.200462344

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NMR Spectroscopic Detection of Protein Protons and Longitudinal Relaxation Rates between 0.01 and 50 MHz

Journal article published in 2005 by Ivano Bertini, Ivano Bertini Prof, Yogesh K. Gupta, Claudio Luchinat ORCID, Claudio Luchinat Prof, Giacomo Parigi Dr, Giacomo Parigi, Christian Schlörb, Harald Schwalbe ORCID, Harald Schwalbe Prof
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This paper is available in a repository.

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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.