Nuclear spin relaxation is a powerful method for studying molecular dynamics at atomic resolution. Recent methods development in biomolecular NMR spectroscopy has enabled detailed investigations of molecular dynamics that are critical for biological function, with prominent examples addressing allostery, enzyme catalysis, and protein folding. Dynamic processes with similar correlation times are often detected in multiple locations of the molecule, raising the question of whether the underlying motions are correlated (corresponding to concerted fluctuations involving many atoms distributed across extended regions of the molecule) or uncorrelated (corresponding to independent fluctuations involving few atoms in localized regions). Here, we ha...
Functionally relevant conformational states of intrinsically disordered proteins (IDPs) are typicall...
Transverse relaxation dispersion NMR spectroscopy can provide atom-specific information about time s...
Intrinsically disordered proteins and intrinsically disordered regions (IDRs) are ubiquitous in the ...
Binding of calcium to the protein calmodulin leads to molecular reorganization that enables interact...
International audience ; Multiple quantum relaxation in proteins reveals unexpected relationships be...
Among the numerous contributions of Geoffrey Bodenhausen to NMR spectroscopy, his developments in th...
AbstractIntrinsically disordered proteins and intrinsically disordered regions (IDRs) are ubiquitous...
Multiple-quantum spin relaxation is a sensitive probe for correlated conformational exchange dynamic...
The dominant dynamics of a partially folded A-state analogue of ubiquitin that give rise to NMR 15N ...
International audienceIntrinsically disordered proteins and intrinsically disordered regions (IDRs) ...
International audienceThe dynamic modes and time scales sampled by intrinsically disordered proteins...
International audienceNuclear magnetic resonance (NMR) spectroscopy is one of the most powerful expe...
Since many biological processes occur on the μs to ms time scale, internal dynamics on that time sca...
International audienceOverwhelming evidence now illustrates the defining role of atomic-scale protei...
The presented thesis work is concerned with the study of molecular dynamics using liquid nuclear mag...
Functionally relevant conformational states of intrinsically disordered proteins (IDPs) are typicall...
Transverse relaxation dispersion NMR spectroscopy can provide atom-specific information about time s...
Intrinsically disordered proteins and intrinsically disordered regions (IDRs) are ubiquitous in the ...
Binding of calcium to the protein calmodulin leads to molecular reorganization that enables interact...
International audience ; Multiple quantum relaxation in proteins reveals unexpected relationships be...
Among the numerous contributions of Geoffrey Bodenhausen to NMR spectroscopy, his developments in th...
AbstractIntrinsically disordered proteins and intrinsically disordered regions (IDRs) are ubiquitous...
Multiple-quantum spin relaxation is a sensitive probe for correlated conformational exchange dynamic...
The dominant dynamics of a partially folded A-state analogue of ubiquitin that give rise to NMR 15N ...
International audienceIntrinsically disordered proteins and intrinsically disordered regions (IDRs) ...
International audienceThe dynamic modes and time scales sampled by intrinsically disordered proteins...
International audienceNuclear magnetic resonance (NMR) spectroscopy is one of the most powerful expe...
Since many biological processes occur on the μs to ms time scale, internal dynamics on that time sca...
International audienceOverwhelming evidence now illustrates the defining role of atomic-scale protei...
The presented thesis work is concerned with the study of molecular dynamics using liquid nuclear mag...
Functionally relevant conformational states of intrinsically disordered proteins (IDPs) are typicall...
Transverse relaxation dispersion NMR spectroscopy can provide atom-specific information about time s...
Intrinsically disordered proteins and intrinsically disordered regions (IDRs) are ubiquitous in the ...