Exploring translocation of proteins on DNA by NMR
Exploring translocation of proteins on DNA by NMR
Abstract While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that three processes are involved in the search procedure: jumping by dissociation of the protein from the DNA followed by re-association at another site,...
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08-22-2011 05:22 AM
Exploring translocation of proteins on DNA by NMR.
Exploring translocation of proteins on DNA by NMR.
Exploring translocation of proteins on DNA by NMR.
J Biomol NMR. 2011 Aug 17;
Authors: Marius Clore G
Abstract
While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that...
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08-19-2011 02:56 PM
[NMR paper] Insights into the interactions between a drug and a membrane protein target by fluori
Insights into the interactions between a drug and a membrane protein target by fluorine cross-polarization magic angle spinning NMR.
Related Articles Insights into the interactions between a drug and a membrane protein target by fluorine cross-polarization magic angle spinning NMR.
Magn Reson Chem. 2004 Feb;42(2):204-11
Authors: Boland MP, Middleton DA
The fluorinated anti-psychotic drug trifluoperazine (TFP) has been shown to be a K(+)-competitive inhibitor of gastric H(+)/K(+)-ATPase, a membrane-embedded therapeutic target for peptic ulcer...
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11-24-2010 09:25 PM
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
FEBS J. 2010 Sep 3;
Authors: Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone EM, Fattorusso R
PED/PEA-15 (phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes) is a ubiquitously expressed protein and a key regulator of cell growth and glucose metabolism. PED/PEA-15 mediates both homotypic and heterotypic interactions and is constituted by...
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09-10-2010 11:53 PM
[NMR paper] Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spec
Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Related Articles Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Int J Pept Protein Res. 1996 Apr;47(4):282-8
Authors: Katahira R, Flotow H, Thomas G, Nosaka AY
An increase in the rate of protein synthesis is found to be accompanied by phosphorylation of the 40S ribosomal protein S6. Treatment of S6 by cyanogen bromide produced three fragments, and one of the fragments of S6, which is a C-terminal...
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08-22-2010 02:27 PM
[NMR paper] Initiation sites of protein folding by NMR analysis.
Initiation sites of protein folding by NMR analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Initiation sites of protein folding by NMR analysis.
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10600-3
Authors: Freund SM, Wong KB, Fersht AR
Detailed characterization of denatured states of proteins is necessary to understand the interactions that funnel the large number of possible conformations along fast routes for folding. Nuclear magnetic resonance...
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08-22-2010 02:20 PM
NMR studies of translocation of the Zif268 protein between its target DNA sites.
NMR studies of translocation of the Zif268 protein between its target DNA sites.
Related Articles NMR studies of translocation of the Zif268 protein between its target DNA sites.
Biochemistry. 2010 Aug 19;
Authors: Takayama Y, Sahu D, Iwahara J
Zif268 is a zinc-finger protein containing three Cys2-His2-type zinc-finger domains that bind the target DNA sequence GCGTGGGCG in a cooperative manner. In this work, we characterized translocation of the Zif268 protein between its target DNA sites using NMR spectroscopy. The residual dipolar coupling...
NMR Studies of Translocation of the Zif268 Protein between Its Target DNA Sites
Biochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable). 
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