NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
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[NMR paper] Solution NMR study of DNA recognition mechanism of IRF4 protein.
Solution NMR study of DNA recognition mechanism of IRF4 protein.
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Nucleic Acids Symp Ser (Oxf). 2004;(48):105-6
Authors: Ishizaki I, Nomura M, Yamamoto K, Matsuyama T, Mishima M, Kojima C
Transcription factor IRF-4 prefers the DNA sequence including CCGAAA. The consensus sequence of the IRF family proteins is NNGAAA, and all crystal structures indicate the NN region does not interact with IRF proteins directly. Here the sequence preference of IRF-4 was...
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[NMR paper] Design of small volume HX and triple-resonance probes for improved limits of detectio
Design of small volume HX and triple-resonance probes for improved limits of detection in protein NMR experiments.
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J Magn Reson. 2003 Sep;164(1):128-35
Authors: Li Y, Logan TM, Edison AS, Webb A
Three- and four-frequency nuclear magnetic-resonance probes have been designed for the study of small amounts of protein. Both "HX" (1H, X, and 2H channels) and "triple-resonance" (1H, 15N, 13C, and 2H) probes were...
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[NMR paper] Sensitivity-enhanced static 15N NMR of solids by 1h indirect detection.
Sensitivity-enhanced static 15N NMR of solids by 1h indirect detection.
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J Magn Reson. 2001 May;150(1):43-8
Authors: Hong M, Yamaguchi S
A method for enhancing the sensitivity of 15N spectra of nonspinning solids through 1H indirect detection is introduced. By sampling the 1H signals in the windows of a pulsed spin-lock sequence, high-sensitivity 1H spectra can be obtained in two-dimensional (2D) spectra whose indirect dimension yields the 15N chemical...
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[NMR paper] Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the ap
Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment.
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J Biomol NMR. 2001 Mar;19(3):231-41
Authors: Iwahara J, Wojciak JM, Clubb RT
The NMR spectra of the complex between the DNA-binding domain of the Dead ringer protein (DRI-DBD, Gly262-Gly398) and its DNA binding site...
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[NMR paper] A systematic case study on using NMR models for molecular replacement: p53 tetrameriz
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Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1535-40
Authors: Chen YW, Clore GM
Molecular replacement using search models derived from nuclear magnetic resonance (NMR) spectroscopy has often proved problematic. It has been known for some time that the overall differences in atomic positions (r.m.s.d.)...
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Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low c
Clean STD-NMR spectrum for improved detection of ligand-protein interactions at low concentration of protein.
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Magn Reson Chem. 2010 Oct 18;
Authors: Xia Y, Zhu Q, Jun KY, Wang J, Gao X
Saturation transfer difference (STD)-NMR has been widely used to screen ligand compound libraries for their binding activities to proteins and to determine the binding epitopes of the ligands. We report herein, a Clean STD-NMR method...
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10-22-2010 06:02 AM
[NMR paper] High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substra
High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein.
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