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Literature DB >> 22293398

Disordered proteins studied by chemical shifts.

Magnus Kjaergaard¹, Flemming M Poulsen.

Abstract

Entities: Disease

Mesh：

Substances：
Proteins

Year: 2011 PMID： 22293398 DOI： 10.1016/j.pnmrs.2011.10.001

Source DB: PubMed Journal: Prog Nucl Magn Reson Spectrosc ISSN： 0079-6565 Impact factor: 9.795

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Cited

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19 in total

Review 1. Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.

Authors: Jane R Allison
Journal: Biophys Rev Date: 2012-09-01

2. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.

Authors: Wade M Borcherds; Gary W Daughdrill
Journal: Methods Enzymol Date: 2018-10-22 Impact factor: 1.600

3. Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins.

Authors: Wolfgang Bermel; Marta Bruix; Isabella C Felli; Vasantha Kumar M V; Roberta Pierattelli; Soraya Serrano
Journal: J Biomol NMR Date: 2013-01-12 Impact factor: 2.835

4. POTENCI: prediction of temperature, neighbor and pH-corrected chemical shifts for intrinsically disordered proteins.

Authors: Jakob Toudahl Nielsen; Frans A A Mulder
Journal: J Biomol NMR Date: 2018-02-05 Impact factor: 2.835

Review 5. Functions of intrinsic disorder in transmembrane proteins.

Authors: Magnus Kjaergaard; Birthe B Kragelund
Journal: Cell Mol Life Sci Date: 2017-06-10 Impact factor: 9.261

6. Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone 15N or 13C' chemical shifts of multiple contiguous residues in highly resolved 3D spectra.

Authors: Yuichi Yoshimura; Natalia V Kulminskaya; Frans A A Mulder
Journal: J Biomol NMR Date: 2015-01-11 Impact factor: 2.835

Disordered proteins studied by chemical shifts.

Review 1. Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.

2. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.

3. Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins.

4. POTENCI: prediction of temperature, neighbor and pH-corrected chemical shifts for intrinsically disordered proteins.

Review 5. Functions of intrinsic disorder in transmembrane proteins.

6. Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone 15N or 13C' chemical shifts of multiple contiguous residues in highly resolved 3D spectra.

7. Can proteins be intrinsically disordered inside a membrane?

8. Cyclic N-terminal loop of amylin forms non amyloid fibers.

9. Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.

10. In-cell ¹³C NMR spectroscopy for the study of intrinsically disordered proteins.