Resonance Assignments and Secondary Structure Analysis of E. coli Thioredoxin by Magic Angle Spinning Solid-State NMR Spectroscopy-Reference-Cited by-同舟云学术

Resonance Assignments and Secondary Structure Analysis of E. coli Thioredoxin by Magic Angle Spinning Solid-State NMR Spectroscopy

Published:2005-09-01 Issue:38 Volume:109 Page:18135-18145
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

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

Affiliation:

1. Department of Chemistry and Biochemistry, Brown Laboratories, University of Delaware, Newark, Delaware 19716, and Department of Chemistry, Science Building, City College of the City University of New York, New York, New York 10031

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp052774d

Reference62 articles.

1. Measurement of Dipolar Couplings in a Uniformly 13C,15N-Labeled Membrane Protein: Distances between the Schiff Base and Aspartic Acids in the Active Site of Bacteriorhodopsin

2. Oligomeric β-Structure of the Membrane-Bound HIV-1 Fusion Peptide Formed from Soluble Monomers

3. Perturbation of the Hydrophobic Core of Lipid Bilayers by the Human Antimicrobial Peptide LL-37

4. Solid-State NMR Investigation of the Selective Perturbation of Lipid Bilayers by the Cyclic Antimicrobial Peptide RTD-1

5. Site-Directed Rotational Resonance Solid-State NMR Distance Measurements Probe Structure and Mechanism in the Transmembrane Domain of the Serine Bacterial Chemoreceptor

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