A method for solution NMR structural studies of large integral membrane proteins: Reverse micelle encapsulation-Reference-Cited by-同舟云学术

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A method for solution NMR structural studies of large integral membrane proteins: Reverse micelle encapsulation

Published:2010-02 Issue:2 Volume:1798 Page:150-160
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Kielec Joseph M.,Valentine Kathleen G.,Wand A. Joshua

Funder

Mathers Foundation

National Institutes of Health (NIH)

National Science Foundation

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference44 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;Pervushin;Proc. Natl. Acad. Sci. U. S. A.,1997

2. High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids;Wand;Proc. Natl. Acad. Sci. U. S. A.,1998

3. Cold denaturation of encapsulated ubiquitin;Pometun;J. Am. Chem. Soc.,2006

4. Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation;Babu;Nat. Struct. Mol. Biol.,2004

5. Forced folding and structural analysis of metastable proteins;Peterson;J. Am. Chem. Soc.,2004

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