Application of One-Dimensional Dipolar Shift Solid-State NMR Spectroscopy To Study the Backbone Conformation of Membrane-Associated Peptides in Phospholipid Bilayers-Reference-Cited by-同舟云学术

Application of One-Dimensional Dipolar Shift Solid-State NMR Spectroscopy To Study the Backbone Conformation of Membrane-Associated Peptides in Phospholipid Bilayers

Published:1999-09-01 Issue:39 Volume:103 Page:8383-8390
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Lee D. K.¹,Santos J. S.¹,Ramamoorthy A.¹

Affiliation:

1. Biophysics Research Division and Department of Chemistry, The University of Michigan, Ann Arbor, Michigan 48109-1055

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/jp9914929

Reference61 articles.

1. Solid-state NMR structural studies of peptides and proteins in membranes

2. Ramamoorthy, A.; Marassi, F. M.; Opella, S. J. InProceedings of theInternational School of Biological Magnetic Resonance, 2nd Course,Dynamics and the Problem of Recognition in Biological Macromolecules;Jardetsky, O., Lefeure,J., Eds.; Plenum: New York, 1996; Chapter 17, pp 237−255.

3. Magic angle spinning NMR spectroscopy of membrane proteins

4. Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers

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