NMR contributions to structural dynamics studies of intrinsically disordered proteins

By R. Konrat. 2014

172 citations recorded by the source corpus.

Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This article will summarize key advances in basic physical-chemistry and NMR methodology, outline their limitations and envision future R&D directions.

Subfields: Molecular Biology, Nuclear and High Energy Physics, Spectroscopy

How researchers see this paper

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

In Molecular Biology

1. Kuldip K. Paliwal
2. Jack Hanson
3. Yaoqi Zhou
4. Thomas Litfin
5. Richard W. Kriwacki
6. Diana M. Mitrea
7. Yuedong Yang
8. Jinbo Xu

In Nuclear and High Energy Physics

1. Jack Hanson
2. Richard W. Kriwacki
3. Diana M. Mitrea
4. Yaoqi Zhou
5. Kuldip K. Paliwal

In Spectroscopy

1. Thomas Litfin
2. Jack Hanson
3. Richard W. Kriwacki
4. Diana M. Mitrea
5. Yaoqi Zhou
6. Kuldip K. Paliwal

Citations in the corpus

• SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “…monetary and time cost of experimental procedures, such as nuclear magnetic resonance (NMR), X-ray crystallography, and circular dichroism (CD) [12,13], many computational methods have been designed to bridge the growing gap between unannotated and annotated protein structures and/or their…”
• Principles of protein structural ensemble determination. (2017, unknown): “commonly used to characterize protein conformational fluctuations, and it has also recently been recognized for X-ray crystallography [15 ,16].”
• Phase separation in biology; functional organization of a higher order (2016, background): “Furthermore, longrange structure within disordered proteins can be studied using paramagnetic relaxation enhancement (PRE) methods and through the measurement of residual dipolar couplings [86].”