NMR structure of oxidizedEscherichia coliglutaredoxin: Comparison with reducedE. coliglutaredoxin and functionally related proteins-Reference-Cited by-同舟云学术

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NMR structure of oxidizedEscherichia coliglutaredoxin: Comparison with reducedE. coliglutaredoxin and functionally related proteins

Published:1992-03 Issue:3 Volume:1 Page:310-321
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Xia Tai-He,Bushweller John H.,Sodano Patrick,Billeter Martin,Björnberg Olof,Holmgren Arne,Wüthrich Kurt

Funder

Schweizerischer Nationalfonds

Swedish Cancer Society

Karolinska Institute

US National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560010302/fullpdf

Reference32 articles.

1. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules;Anil-Kumar;Biochem. Biophys. Res. Commun.,1980

2. Comparison of the high-resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals;Billeter;J. Mol. Biol.,1989

3. Determination of the three-dimensional structure of the antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy;Billeter;J. Mol. Biol.,1990

4. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy;Bodenhausen;Chem. Phys. Lett.,1980

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