[NMR paper] Toward an integrated model of protein-DNA recognition as inferred from NMR studies on
Toward an integrated model of protein-DNA recognition as inferred from NMR studies on the Lac repressor system.
Related Articles Toward an integrated model of protein-DNA recognition as inferred from NMR studies on the Lac repressor system.
Chem Rev. 2004 Aug;104(8):3567-86
Authors: Kalodimos CG, Boelens R, Kaptein R
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[NMR paper] Design of a functional protein for molecular recognition: specificity of ligand bindi
Design of a functional protein for molecular recognition: specificity of ligand binding in a metal-assembled protein cavity probed by 19f NMR.
Related Articles Design of a functional protein for molecular recognition: specificity of ligand binding in a metal-assembled protein cavity probed by 19f NMR.
J Am Chem Soc. 2004 Apr 7;126(13):4192-8
Authors: Doerr AJ, Case MA, Pelczer I, McLendon GL
A metal-assembled homotrimeric coiled coil based on the GCN4-p1 sequence has been designed that noncovalently binds hexafluorobenzene and other similar...
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11-24-2010 09:51 PM
[NMR paper] Solution NMR study of DNA recognition mechanism of IRF4 protein.
Solution NMR study of DNA recognition mechanism of IRF4 protein.
Related Articles Solution 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...
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[NMR paper] Protein structural motif recognition via NMR residual dipolar couplings.
Protein structural motif recognition via NMR residual dipolar couplings.
Related Articles Protein structural motif recognition via NMR residual dipolar couplings.
J Am Chem Soc. 2001 Feb 14;123(6):1222-9
Authors: Andrec M, Du P, Levy RM
NMR residual dipolar couplings have great potential to provide rapid structural information for proteins in the solution state. This information even at low resolution may be used to advantage in proteomics projects that seek to annotate large numbers of gene products for entire genomes. In this paper, we...
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11-19-2010 08:32 PM
[NMR paper] Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immuno
Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor.
Related Articles Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor.
J Biol Chem. 2000 May 26;275(21):16174-82
Authors: Gaul BS, Harrison ML, Geahlen RL, Burton RA, Post CB
The immunoreceptor tyrosine-based activation motif (ITAM) plays a central role...
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11-18-2010 09:15 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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[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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[NMR paper] Enhanced protein fold recognition using secondary structure information from NMR.
Enhanced protein fold recognition using secondary structure information from NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Enhanced protein fold recognition using secondary structure information from NMR.
Protein Sci. 1999 May;8(5):1127-33
Authors: Ayers DJ, Gooley PR, Widmer-Cooper A, Torda AE
NMR offers...