[NMR paper] The Three Dimensional Structure and Interaction Studies of HCV p7 in DHPC by Solution NMR.
The Three Dimensional Structure and Interaction Studies of HCV p7 in DHPC by Solution NMR.
The Three Dimensional Structure and Interaction Studies of HCV p7 in DHPC by Solution NMR.
Biochemistry. 2013 Jul 10;
Authors: Cook GA, Dawson LA, Tian Y, Opella SJ
Abstract
Hepatitis C Virus (HCV) protein p7 plays an important role in the assembly and release of mature virus particles. This small 63-residue membrane protein has been shown to induce channel activity, which may contribute to its functions. p7 is highly conserved throughout the...
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[NMR paper] Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I fro
Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803.
Related Articles Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803.
Biochemistry. 2002 Nov 26;41(47):13902-14
Authors: Barth P, Savarin P, Gilquin B, Lagoutte B, Ochsenbein F
PsaE is a small peripheral subunit of photosystem I (PSI) that is very accessible to the surrounding medium. It plays an essential role in optimizing the interactions with the soluble electron...
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11-24-2010 08:58 PM
[NMR paper] Lipid-protein interactions in DHPC micelles containing the integral membrane protein
Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.
Related Articles Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13533-7
Authors: Fernández C, Hilty C, Wider G, Wüthrich K
Intermolecular nuclear Overhauser effects (NOEs) between the integral outer membrane protein OmpX from Escherichia coli and dihexanoylphosphatidylcholine (DHPC) provided a detailed...
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Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.
Related Articles Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 26;
Authors: Schanda P, Meier BH, Ernst M
Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and accurate measurement protocols, which are not yet fully developed. In this study, we investigate the backbone dynamics of microcrystalline ubiquitin...
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10-29-2010 07:05 PM
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy
Paul Schanda, Beat H. Meier and Matthias Ernst
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja100726a/aop/images/medium/ja-2010-00726a_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja100726a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/vMvBmzNs148
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[NMR paper] Molecular dynamics-derived conformation and intramolecular interaction analysis of th
Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
Related Articles Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
...
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[NMR paper] Molecular dynamics simulation of E. coli ribonuclease H1 in solution: correlation wit
Molecular dynamics simulation of E. coli ribonuclease H1 in solution: correlation with NMR and X-ray data and insights into biological function.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Molecular dynamics simulation of E. coli ribonuclease H1 in solution: correlation with NMR and X-ray data and insights into biological function.
J Mol Biol. 1995 Dec 8;254(4):771-92
Authors: Philippopoulos M, Lim C
A 500 ps molecular dynamics simulation of Escherichia coli RNase...
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[NMR paper] Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse
Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Related Articles Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Biochemistry. 1990 Aug 14;29(32):7387-401
Authors: Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM
The backbone dynamics of uniformly 15N-labeled interleukin-1 beta are investigated by using two-dimensional inverse detected heteronuclear 15N-1H NMR...