Výsledky vyhledávání - "R W, Strange"

XAFS study of the high-affinity copper-binding site of human PrP(91-231) and its low-resolution structure in solution

Autor: S S, Hasnain, L M, Murphy, R W, Strange, J G, Grossmann, A R, Clarke, G S, Jackson, J, Collinge

Publikováno v: Journal of molecular biology. 311(3)

Here, we describe the structure of a C-terminal high-affinity copper-binding site within a truncated recombinant human PrP containing residues 91-231, which lacks the octapeptide repeat region. We show that at least two extra co-ordinating groups are

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::900439ddca2b13e90ca6d1141d502121
https://pubmed.ncbi.nlm.nih.gov/11493001

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Copper K-extended x-ray absorption fine structure studies of oxidized and reduced dopamine beta-hydroxylase. Confirmation of a sulfur ligand to copper(I) in the reduced enzyme

Autor: N J, Blackburn, S S, Hasnain, T M, Pettingill, R W, Strange

Publikováno v: The Journal of biological chemistry. 266(34)

The structure of the copper sites in oxidized and reduced dopamine beta-hydroxylase has been studied by extended x-ray absorption fine structure spectroscopy using a restrained refinement approach to data analysis. An histidine-rich active site has b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::99ad77c9b496f95da83d02911d4250b2
https://pubmed.ncbi.nlm.nih.gov/1744110

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Carbonmonoxy dopamine beta-hydroxylase. Structural characterization by Fourier transform infrared, fluorescence, and x-ray absorption spectroscopy

Autor: T M, Pettingill, R W, Strange, N J, Blackburn

Publikováno v: The Journal of biological chemistry. 266(26)

The carbon monoxide complex of ascorbate-reduced dopamine beta-hydroxylase has been prepared and characterized by Fourier transform infrared, fluorescence, and x-ray absorption spectroscopies. CO has previously been shown to be a competitive inhibito

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::eb78098264977bb9392edef49f6ad1f9
https://pubmed.ncbi.nlm.nih.gov/1894598

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Evidence from extended X-ray absorption fine structure and site-specific mutagenesis for zinc fingers in UvrA protein of Escherichia coli

Autor: S, Navaratnam, G M, Myles, R W, Strange, A, Sancar

Publikováno v: The Journal of biological chemistry. 264(27)

The UvrA protein is the damage recognition subunit of the Escherichia coli repair enzyme ABC excision nuclease. Sequence analysis of this 940-amino acid protein revealed two regions of sequence homology to the zinc finger motif found in many DNA bind

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ece9e7075c92ab0404c6a113c5f0cc1a
https://pubmed.ncbi.nlm.nih.gov/2550431

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