Related ArticlesNMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY.
Biochemistry. 1995 Sep 19;34(37):11998-2004
Authors: Werner MH, Bianchi ME, Gronenborn AM, Clore GM
The conformation of an eight base pair DNA oligonucleotide duplex bound to the human testis determining factor SRY and the orientation of the protein domain within the complex have been analyzed by a variety of NMR methods which permit the selective observation of protons attached to 12C nuclei in the presence of uniformly enriched 13C/15N protein. Qualitative analysis of nuclear and rotating frame Overhauser enhancement spectra at multiple mixing times indicates that the conformation of the SRY-bound DNA is distinct from that of A- and B-DNA, in agreement with the recent three-dimensional structure determination of the complex [Werner, M. W., Huth, J. R., Gronenborn, A. M., & Clore, G. M. (1995) Cell 81, 705-714]. Selective observation of intermolecular NOEs between protein and DNA indicates that partial intercalation of a protein side chain occurs between two adenine bases in the DNA octamer. The analysis of structural features by NMR for this unusual DNA conformer and the orientation of the protein domain on the DNA is discussed. The structural features of the DNA complexed to SRY are remarkably similar, but not identical, to those of DNA complexed to the TATA-binding protein (TBP).
[NMR paper] NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM pr
NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Related Articles NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Protein Eng. 2003 Apr;16(4):247-54
Authors: Shimizu M, Hiroaki H, Kohda D, Hosoya T, Akiyama-Oda Y, Hotta Y, Morita EH, Morikawa K
Drosophila GCM (glial cell missing) is a novel DNA-binding protein that determines the fate of glial precursors from the neural default to glia....
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[NMR paper] Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fra
Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fragment containing the ERCC1-binding region and the minimal DNA-binding domain (M59-F219).
Related Articles Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fragment containing the ERCC1-binding region and the minimal DNA-binding domain (M59-F219).
Mutat Res. 2001 Jun 5;486(1):1-10
Authors: Buchko GW, Isern NG, Spicer LD, Kennedy MA
XPA is a central protein component of nucleotide excision repair (NER), a ubiquitous,...
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[NMR paper] Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation o
Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR.
Related Articles Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR.
Biochemistry. 2000 Nov 28;39(47):14472-80
Authors: Kawase Y, Tanio M, Kira A, Yamaguchi S, Tuzi S, Naito A, Kataoka M, Lanyi JK, Needleman R, Saitô H
According to previous X-ray diffraction studies, the D85N mutant of...
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[NMR paper] 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes
31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Related Articles 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Eur J Biochem. 2000 Feb;267(4):1223-9
Authors: Castagné C, Murphy EC, Gronenborn AM, Delepierre M
Complexes of the HMG box protein SRY with two duplexes of 8 and 14 base pairs have been studied by 31P NMR and complete assignment of all phosphorus signals of the bound DNA duplexes are presented. While for the free DNA, all 31P signals display limited...
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[NMR paper] pH-induced structural changes in human serum apotransferrin. pKa values of histidine
pH-induced structural changes in human serum apotransferrin. pKa values of histidine residues and N-terminal amino group determined by 1H-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles pH-induced structural changes in human serum apotransferrin. pKa values of histidine residues and N-terminal amino group determined by 1H-NMR spectroscopy.
Eur J Biochem. 1994 Mar 15;220(3):781-7
Authors: Kubal G, Sadler PJ, Tucker A
...
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[NMR paper] Oxalate- and Ga(3+)-induced structural changes in human serum transferrin and its rec
Oxalate- and Ga(3+)-induced structural changes in human serum transferrin and its recombinant N-lobe. 1H NMR detection of preferential C-lobe Ga3+ binding.
Related Articles Oxalate- and Ga(3+)-induced structural changes in human serum transferrin and its recombinant N-lobe. 1H NMR detection of preferential C-lobe Ga3+ binding.
Biochemistry. 1993 Apr 6;32(13):3387-95
Authors: Kubal G, Mason AB, Patel SU, Sadler PJ, Woodworth RC
(1) The binding of the synergistic anion oxalate and Ga3+ to human serum transferrin (HTF, 80 kDa) and its recombinant...
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[NMR paper] 1H NMR spectroscopic studies on the interactions between human plasma antithrombin II
1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Related Articles 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Biochemistry. 1992 Mar 3;31(8):2286-94
Authors: Horne A, Gettins P
The effects of length and composition upon the antithrombin-binding properties of heparin have been investigated for two series of structurally related heparin oligosaccharides. Each...
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[NMR paper] Cephaloridine-induced nephrotoxicity in the Fischer 344 rat: proton NMR spectroscopic
Cephaloridine-induced nephrotoxicity in the Fischer 344 rat: proton NMR spectroscopic studies of urine and plasma in relation to conventional clinical chemical and histopathological assessments of nephronal damage.
Related Articles Cephaloridine-induced nephrotoxicity in the Fischer 344 rat: proton NMR spectroscopic studies of urine and plasma in relation to conventional clinical chemical and histopathological assessments of nephronal damage.
Arch Toxicol. 1992;66(8):525-37
Authors: Anthony ML, Gartland KP, Beddell CR, Lindon JC, Nicholson JK
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