Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations-Reference-Cited by-同舟云学术

Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations

Published:2015 Issue:43 Volume:17 Page:28789-28801
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Paluch Piotr¹²³⁴,Pawlak Tomasz¹²³⁴^ORCID,Jeziorna Agata¹²³⁴,Trébosc Julien⁵⁶⁷⁸⁹,Hou Guangjin¹⁰¹¹¹²¹³,Vega Alexander J.¹⁰¹¹¹²¹³,Amoureux Jean-Paul⁵⁶⁷⁸⁹,Dracinsky Martin¹⁴¹⁵¹⁶¹⁷,Polenova Tatyana¹⁰¹¹¹²¹³,Potrzebowski Marek J.¹²³⁴

Affiliation:

1. Polish Academy of Sciences

2. Centre of Molecular and Macromolecular Studies

3. PL-90-363 Łodz

4. Poland

5. Unit of Catalysis and Chemistry of Solids (UCCS)

6. CNRS-8181

7. University Lille North of France

8. 59652 Villeneuve d'Ascq

9. France

10. Department of Chemistry and Biochemistry

11. University of Delaware

12. Newark

13. USA

14. Institute of Organic Chemistry and Biochemistry

15. AS CR

16. Prague

17. Czech Republic

Abstract

We report a new NMR methodology, which provides detailed probe of molecular motions occurring on timescales of nano- to microseconds, in sidechains of proteins.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CP/C5CP04475H

Reference55 articles.

1. Solid-State NMR Spectroscopy on Complex Biomolecules

2. Solid-State NMR-Based Approaches for Supramolecular Structure Elucidation

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4. Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy

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