Unfolded proteins and protein folding studied by NMR.
By H. J. Dyson, Peter E. Wright. Chemical Reviews, 2004
639 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/4457647a90ce738008f03d447c7095bc534e0c41
How researchers see this paper
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In Materials Chemistry
- Burkhard Rost
- Avner Schlessinger
- Jinfeng Liu
- M. Grimaldo
- F. Roosen‐Runge
- Peter Tompa
- Fajun Zhang
- John R. Engen
In Molecular Biology
- Burkhard Rost
- Avner Schlessinger
- Jinfeng Liu
- Lukasz Kurgan
- Vladimir N Uversky
- Zhenling Peng
- Christian Schaefer
- M. Grimaldo
Citations in the corpus
- The interplay between structure and function in intrinsically unstructured proteins (2005, background): “dynamics of IUPs, provides structural information via secondary chemical shift, residual dipolar coupling and long-range NOE upon spin labeling [19].”
- Natively Unstructured Loops Differ from Other Loops (2007, background): “(NMR) spectroscopy, X-ray crystallography, or proteolysis experiments [7–9].”
- NMR contributions to structural dynamics studies of intrinsically disordered proteins (2014, positive): “Hydrogen exchange rates, NMR chemical shifts and residual dipolar couplings (RDC) can be used to evaluate local transient secondary structure elements with atomic resolution, whereas paramagnetic relaxation enhancement (PRE) reports on transient long-range contacts [1].”
- Hydrogen exchange mass spectrometry for the analysis of protein dynamics. (2006, methodology): “Traditionally, hydrogen exchange methodology has been used in conjunction with NMR analysis [see (Dyson & Wright, 2004) for a review].”
- Dynamics of proteins in solution (2019, methodology): “We refer the reader to reviews from the last decade for a more detailed overview (Dosset et al., 2000; Ishima and Torchia, 2000; Dyson and Wright, 2004; Blackledge, 2005; Kay, 2005; Boehr et al., 2006; Mittermaier and Kay, 2009; Kleckner and Foster, 2011; Krushelnitsky et al., 2013).”
- Protein flexibility and rigidity predicted from sequence (2005, methodology): “Solution NMR spectroscopy methods are commonly used to characterize the dynamic properties of proteins.(21,51,52) It has been previously shown that order parameter data obtained from NMR spin relaxation experiments are, to an extent, correlated with experimental B-value data.”