New Tools Provide New Insights in NMR Studies of Protein Dynamics

By A. Mittermaier, Lewis E. Kay. Science, 2006

716 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/f7efc5412f6dabb96506dc27ad6902bfe9283cd8

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Michele Vendruscolo
2. K. Henzler-Wildman
3. Hue Sun Chan
4. Piero Fariselli
5. Pietro Sormanni
6. Dorothee Kern

In Molecular Biology

1. K. Henzler-Wildman
2. Michele Vendruscolo
3. E. Bornberg-Bauer
4. Richard Wroe
5. Peng Sang
6. Hue Sun Chan
7. Piero Fariselli
8. Carlo Camilloni

In Spectroscopy

1. Michele Vendruscolo
2. K. Henzler-Wildman
3. B. L. de Groot
4. Dorothee Kern

Citations in the corpus

• Dynamic personalities of proteins (2007, methodology): “Dynamic information is extracted from relaxation of nuclei after excitation, using a variety of NMR experiments to span dynamics on timescales from picoseconds to seconds and to assess several types of nucleus ( 1 H, 2 H, 13 C and 15 N) site specificall”
• The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins. (2015, background): “Proteins folded in their native states experience conformational fluctuations, which in many cases facilitate their functions [1–6].”
• Insights into Protein–Ligand Interactions: Mechanisms, Models, and Methods (2016, background): “For example, X-ray-diffraction data contain information not only about the enthalpic contribution (intermolecular noncovalent interactions) but also about some entropic contribution (spatial distribution around the average structure as reflected by the B-factors) [21,55]; NMR methods have the advant”
• A structural model of latent evolutionary potentials underlying neutral networks in proteins (2007, background): “Experimentally, as is emphasized in the “new view of protein structures,” biomolecules are dynamic entities (Mittermaier and Kay, 2006), with many minor structural fluctuations even for cooperatively folding proteins under native conditions (Bai et al.”
• Detection of Functional Modes in Protein Dynamics (2009, background): “[3,4], X-ray crystallography [5], as well as single-molecule fluorescence [6] or electron-transfer measurements [7].”