Solution NMR structure of the cold‐shock protein from the hyperthermophilic bacterium <i>Thermotoga maritima</i>
Werner Kremer(University of Regensburg), Hans Robert Kalbitzer, Benjamin Schuler(University of Zurich), Wolfram Gronwald(University of Regensburg), Stefan Harrieder(University of Regensburg), Christine Welker(University of Regensburg), Matthias Geyer(University of Bonn), Rainer Jaenicke(University of Regensburg)
Cited by 102
Related Papers
Extreme disorder in an ultrahigh-affinity protein complex
|Nature|2018|685
Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study
|Nature Methods|2018|527
Extreme dynamics in a biomolecular condensate
|Nature|2023|349
Combined chemical shift changes and amino acid specific chemical shift mapping of protein–protein interactions
|Journal of Biomolecular NMR|2007|236
Advances in amino acid analysis
|Analytical and Bioanalytical Chemistry|2008|235