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

doi:10.1002/anie.200462344

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 journal › Article › peer-review

30 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 language	English
Pages (from-to)	2223-2225
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	44
Issue number	15
DOIs	https://doi.org/10.1002/anie.200462344
State	Published - 8 Apr 2005
Externally published	Yes

Keywords

Aggregation
Deuterium
Protein folding
Protein structures
Protonation

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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.",

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AU - Bertini, Ivano

AU - Gupta, Yogesh K.

AU - Luchinat, Claudio

AU - Parigi, Giacomo

AU - Schlörb, Christian

AU - Schwalbe, Harald

PY - 2005/4/8

Y1 - 2005/4/8

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AB - (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.

KW - Aggregation

KW - Deuterium

KW - Protein folding

KW - Protein structures

KW - Protonation

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JF - Angewandte Chemie - International Edition

IS - 15

ER -

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

Abstract

Keywords

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