A missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 A resolution
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Inner- and outer-sphere metal coordination in blue copper proteinsStructure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasisRationally tuning the reduction potential of a single cupredoxin beyond the natural rangeThe 1.4 Å resolution structure ofParacoccus pantotrophuspseudoazurinThe sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper siteModular Artificial CupredoxinsRack-induced metal binding vs. flexibility: Met121His azurin crystal structures at different pHBlue copper proteins: a comparative analysis of their molecular interaction properties.Novel types of two-domain multi-copper oxidases: possible missing links in the evolution.Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on Förster resonance energy transfer techniques.Comparative analysis of the phytocyanin gene family in 10 plant species: a focus on Zea mays.Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form.Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: plant-specific mononuclear blue copper proteins.Spectroscopic and DFT studies of second-sphere variants of the type 1 copper site in azurin: covalent and nonlocal electrostatic contributions to reduction potentials.Outer-sphere contributions to the electronic structure of type zero copper proteinsThermus oshimai JL-2 and T. thermophilus JL-18 genome analysis illuminates pathways for carbon, nitrogen, and sulfur cycling.Axial interactions in the mixed-valent CuA active site and role of the axial methionine in electron transfer.NMR hyperfine shifts in blue copper proteins: a quantum chemical investigation.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersCupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes.Defining the metal specificity of a multifunctional biofilm adhesion protein.Copper(I) and nickel(II) complexes with 1:1 vs. 1:2 coordination of ferrocenyl hydrazone ligands: do the geometry and composition of complexes affect DNA binding/cleavage, protein binding, antioxidant and cytotoxic activities?Anisotropic covalency contributions to superexchange pathways in type one copper active sites.Alkaline transition of phytocyanins: a comparison of stellacyanin and umecyanin.The putative phytocyanin genes in Chinese cabbage (Brassica rapa L.): genome-wide identification, classification and expression analysis.Resolving ligand hyperfine couplings of type 1 and 2 Cu(II) in ascorbate oxidase by high field pulse EPR correlation spectroscopy.Prediction of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A genomic analysis.An axial met ligand at a type 1 copper site is preferable for fast electron transfer.Structure and molecular evolution of multicopper blue proteins.
P2860
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P2860
A missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 A resolution
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
A missing link in cupredoxins: ...... ellacyanin at 1.6 A resolution
@ast
A missing link in cupredoxins: ...... ellacyanin at 1.6 A resolution
@en
type
label
A missing link in cupredoxins: ...... ellacyanin at 1.6 A resolution
@ast
A missing link in cupredoxins: ...... ellacyanin at 1.6 A resolution
@en
prefLabel
A missing link in cupredoxins: ...... ellacyanin at 1.6 A resolution
@ast
A missing link in cupredoxins: ...... ellacyanin at 1.6 A resolution
@en
P2093
P2860
P356
P1433
P1476
A missing link in cupredoxins: ...... ellacyanin at 1.6 A resolution
@en
P2093
A M Nersissian
D Eisenberg
J S Valentine
R G Herrmann
R M Nalbandyan
P2860
P304
P356
10.1002/PRO.5560051104
P577
1996-11-01T00:00:00Z