Zobrazeno 1 - 7
of 7
pro vyhledávání: '"K J, Lumb"'
Publikováno v:
Proteins. 43(2)
TFIIA contributes to transcription initiation by stabilizing the TBP-TATA interaction and by mediating the response to transcriptional activators and inhibitors. TFIIA contains a six-stranded beta-sheet domain and a four-helix bundle. The beta-domain
Autor:
E A, Bienkiewicz, K J, Lumb
Publikováno v:
Journal of biomolecular NMR. 15(3)
The 1H, 13C, 15N and 31P random-coil chemical shifts and phosphate pKa values of phosphorylated amino acids pSer, pThr and pTyr in the protected peptide Ac-Gly-Gly-X-Gly-Gly-NH2 have been obtained in water at 25 degrees C over the pH range 2 to 9. An
Autor:
S P, Mestas, K J, Lumb
Publikováno v:
Nature structural biology. 6(7)
Publikováno v:
Science (New York, N.Y.). 271(5252)
Publikováno v:
Journal of molecular biology. 235(3)
Two-dimensional 1H nuclear magnetic resonance spectroscopy has been used to examine the complexes formed in solution between hen egg-white lysozyme and N-acetylglucosamine (GlcNAc) oligosaccharides. Changes in chemical shift have been measured for re
Autor:
K J, Lumb, C M, Dobson
Publikováno v:
Journal of molecular biology. 227(1)
The interaction between hen lysozyme and urea has been investigated using 1H nuclear magnetic resonance spectroscopy. Chemical shift changes for resonances of a number of residues in the vicinity of the active site of the protein have been observed i
Autor:
K J, Lumb, R T, Aplin, S E, Radford, D B, Archer, D J, Jeenes, N, Lambert, D A, MacKenzie, C M, Dobson, G, Lowe
Publikováno v:
FEBS letters. 296(2)
The production of a mutant hen lysozyme is described in which Asp-52, one of the catalytically important residues, is replaced by Ser. The mutant enzyme has very low catalytic activity but NMR studies show that its structure is closely similar to tha