Related ArticlesSolution NMR study of DNA recognition mechanism of IRF4 protein.
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 investigated by NMR and fluorescence antisotropy as an example of the indirect sequence recognition. The 1H-15N HSQC spectra of the IRF-4/DNA complex containing the CCGAAA sequence indicated that the 1:1 complex was formed. The dissociation constants (Kd) for two DNA oligomers containing CCGAAA and GGGAAA were determined by fluorescence antistropy, but their difference was very small.
Systematic Study of Protein Detection Mechanism of Self-Assembling 19F NMR/MRI Nanoprobes toward Rational Design and Improved Sensitivity
Systematic Study of Protein Detection Mechanism of Self-Assembling 19F NMR/MRI Nanoprobes toward Rational Design and Improved Sensitivity
Yousuke Takaoka, Keishi Kiminami, Keigo Mizusawa, Kazuya Matsuo, Michiko Narazaki, Tetsuya Matsuda and Itaru Hamachi
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203996c/aop/images/medium/ja-2011-03996c_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203996c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/fqTSjFalrGg
nmrlearner
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07-12-2011 08:16 AM
[NMR paper] Insights into the mechanism of heterodimerization from the 1H-NMR solution structure
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
Related Articles Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
J Mol Biol. 1998 Aug 7;281(1):165-81
Authors: Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD
The oncoprotein c-Myc (a member of the helix-loop-helix-leucine zipper (b-HLH-LZ) family of transcription factors) must heterodimerize with the b-HLH-LZ Max...
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11-17-2010 11:15 PM
[NMR paper] Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for st
Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Related Articles Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Biochemistry. 1994 Mar 15;33(10):3071-8
Authors: Baleja JD, Mau T, Wagner G
The complex of a monomer of GAL4 with DNA has been investigated by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Previous X-ray analysis has revealed a structure in which a dimer of the N-terminal 65-residue fragment of GAL4 forms a complex,...
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08-22-2010 03:33 AM
[NMR paper] Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for st
Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Related Articles Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Biochemistry. 1994 Mar 15;33(10):3071-8
Authors: Baleja JD, Mau T, Wagner G
The complex of a monomer of GAL4 with DNA has been investigated by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Previous X-ray analysis has revealed a structure in which a dimer of the N-terminal 65-residue fragment of GAL4 forms a complex,...
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08-22-2010 03:33 AM
[NMR paper] Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation
Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
Arch Biochem Biophys. 1993 Mar;301(2):244-50
Authors: Desideri A, Polticelli F, Falconi M, Sette M, Ciriolo MR, Paci M,...
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08-21-2010 11:53 PM
[NMR paper] 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm w
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
Biochim Biophys Acta. 1990 Nov 15;1041(2):186-94
Authors: Hauksson JB, La Mar GN, Pande U, Pandey RK, Parish DW, Singh JP, Smith KM
The...
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08-21-2010 11:04 PM
Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR/x-ray crystallography
Spincore.com are advertising a postdoc NMR position. It sounds pretty interesting.
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Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR /x-ray crystallography
Case Medical School, Cleveland, Ohio, USA
How are signaling events transmitted from one protein to another? To answer this question we are looking to add a postdoctoral co-workers to our interdisciplinary team. Our interest is to understand protein-protein interactions, protein structure and dynamics in the context of cell signaling...
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08-10-2008 02:37 PM
NMR post-doc position: NMR-based dynamics study of enzyme mechanism
The following post-doc position in NMR is available in University of Missouri:
Ad text:
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We have an opening for a postdoctoral fellow to use NMR to study dynamics of an enzyme while it is carrying on reversible catalysis. The prospects are promising and can be compared with thorough enzymology and crystallography of its ligand-dependent conformational changes (done in our dept.). The enzyme is sizeable enough to be challenging, but we have a battery of excellent 800 MHz spectra of deuterated samples for launching the project. The postdoctoral fellow will be housed in a new...