Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR-Reference-Cited by-同舟云学术

Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR

Published:2003-10-08 Issue:1 Volume:555 Page:139-143
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Tamm Lukas K,Abildgaard Frits,Arora Ashish,Blad Heike,Bushweller John H

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(03)01127-X/fullpdf

Reference29 articles.

1. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

2. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins

3. Structure of the outer membrane protein A transmembrane domain

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