Defining Long-Range Order and Local Disorder in Native α-Synuclein Using Residual Dipolar Couplings-Reference-Cited by-同舟云学术

Defining Long-Range Order and Local Disorder in Native α-Synuclein Using Residual Dipolar Couplings

Published:2005-12-01 Issue:51 Volume:127 Page:17968-17969
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Bernadó Pau¹,Bertoncini Carlos W.¹,Griesinger Christian¹,Zweckstetter Markus¹,Blackledge Martin¹

Affiliation:

1. Institute de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF, 41 rue Jules Horowitz, 38027-Grenoble Cedex, France, Department of NMR-Based Structural Biology and Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja055538p

Reference22 articles.

1. Natively unfolded proteins: A point where biology waits for physics

2. Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium

3. NMR structures of biomolecules using field oriented media and residual dipolar couplings

4. Persistence of Native-Like Topology in a Denatured Protein in 8 M Urea

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