Magic Angle Spinning Solid-State NMR Spectroscopy for Structural Studies of Protein Interfaces. Resonance Assignments of Differentially Enriched Escherichia coli Thioredoxin Reassembled by Fragment Complementation-Reference-Cited by-同舟云学术

Magic Angle Spinning Solid-State NMR Spectroscopy for Structural Studies of Protein Interfaces. Resonance Assignments of Differentially Enriched Escherichia coli Thioredoxin Reassembled by Fragment Complementation

Published:2004-11-23 Issue:50 Volume:126 Page:16608-16620
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Marulanda Dabeiba¹,Tasayco Maria Luisa¹,McDermott Ann¹,Cataldi Marcela¹,Arriaran Vilma¹,Polenova Tatyana¹

Affiliation:

1. Contribution from the Department of Chemistry and Biochemistry, Brown Laboratories, University of Delaware, Newark, Delaware 19716, Department of Chemistry, Science Building, City College of the City University of New York, New York, New York 10031, and Department of Chemistry, Havemeyer Hall, Columbia University, New York, New York 10027

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0464589

Reference66 articles.

1. Applications of solid state NMR to the structural characterization of amyloid fibrils: methods and results

2. A structural model for Alzheimer's -amyloid fibrils based on experimental constraints from solid state NMR

3. The Closed State of a H+ Channel Helical Bundle Combining Precise Orientational and Distance Restraints from Solid State NMR

4. Structural Studies of Biomaterials Using Double-Quantum Solid-State NMR Spectroscopy

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