Add to ORKGRecent progress has advanced our abilities to use NMR spectroscopy to follow - in real time - the structural and dynamic changes taking place during protein folding
International audienceOverwhelming evidence now illustrates the defining role of atomic-scale protei...
Protein folding is a highly complex process proceeding through a number of disordered and partially ...
Recent advances in NMR spectroscopy and the availability of high magnetic field strengths now offer ...
SIGLEAvailable from British Library Document Supply Centre- DSC:D187740 / BLDSC - British Library Do...
Pioneering work in the 1980s has established NMR spectroscopy as a routine method for protein struct...
Deciphering the mechanism of protein folding is one of the most desirable goals in the field of stru...
protein folding intermediates Exchange rates of individual amide protons in the polypeptide backbone...
The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinet...
AbstractNMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding,...
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy fo...
Proteins are dynamic molecules that often undergo conformational changes while performing their spec...
International audienceNMR spectroscopy is a powerful tool for studying molecular dynamics at atomic ...
AbstractCharacterization of the mechanisms by which proteins fold into their native conformations is...
Pressure-jump hardware permits direct observation of protein NMR spectra during a cyclically repeate...
Methods for macromolecular structure determination (NMR and crystallography) are now being used to g...
International audienceOverwhelming evidence now illustrates the defining role of atomic-scale protei...
Protein folding is a highly complex process proceeding through a number of disordered and partially ...
Recent advances in NMR spectroscopy and the availability of high magnetic field strengths now offer ...
SIGLEAvailable from British Library Document Supply Centre- DSC:D187740 / BLDSC - British Library Do...
Pioneering work in the 1980s has established NMR spectroscopy as a routine method for protein struct...
Deciphering the mechanism of protein folding is one of the most desirable goals in the field of stru...
protein folding intermediates Exchange rates of individual amide protons in the polypeptide backbone...
The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinet...
AbstractNMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding,...
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy fo...
Proteins are dynamic molecules that often undergo conformational changes while performing their spec...
International audienceNMR spectroscopy is a powerful tool for studying molecular dynamics at atomic ...
AbstractCharacterization of the mechanisms by which proteins fold into their native conformations is...
Pressure-jump hardware permits direct observation of protein NMR spectra during a cyclically repeate...
Methods for macromolecular structure determination (NMR and crystallography) are now being used to g...
International audienceOverwhelming evidence now illustrates the defining role of atomic-scale protei...
Protein folding is a highly complex process proceeding through a number of disordered and partially ...
Recent advances in NMR spectroscopy and the availability of high magnetic field strengths now offer ...