Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
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Identifying important structural characteristics of arsenic resistance proteins by using designed three-stranded coiled coilsStructural Comparisons of Apo- and Metalated Three-Stranded Coiled Coils Clarify Metal Binding Determinants in Thiolate Containing Designed PeptidesHydrolytic catalysis and structural stabilization in a designed metalloproteinCation-pi interactions studied in a model coiled-coil peptided-Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils.Hg(II) binding to a weakly associated coiled coil nucleates an encoded metalloprotein fold: a kinetic analysis.Probing a homoleptic PbS3 coordination environment in a designed peptide using 207Pb NMR spectroscopy: implications for understanding the molecular basis of lead toxicity.Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.Experimental and theoretical evaluation of multisite cadmium(II) exchange in designed three-stranded coiled-coil peptidesThe importance of stereochemically active lone pairs for influencing Pb(II) and As(III) protein bindingExperimental and theoretical characterization of arsenite in water: insights into the coordination environment of As-O.The correlation of 113Cd NMR and 111mCd PAC spectroscopies provides a powerful approach for the characterization of the structure of Cd(II)-substituted Zn(II) proteinsUsing diastereopeptides to control metal ion coordination in proteinsDesigning functional metalloproteins: from structural to catalytic metal sites.Probing the coordination environment of the human copper chaperone HAH1: characterization of Hg(II)-bridged homodimeric species in solution.Arsenic Induction of Metallothionein and Metallothionein Induction Against Arsenic Cytotoxicity.Selective and sensitive turn-on fluorescent sensing of arsenite based on cysteine fused tetraphenylethene with AIE characteristics in aqueous media.Incorporation of second coordination sphere D-amino acids alters Cd(II) geometries in designed thiolate-rich proteins.Lead(II) Binding in Natural and Artificial Proteins.Immobilization of As(V) in Rhizopus oryzae Investigated by Batch and XAFS Techniques.
P2860
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P2860
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
@ast
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
@en
type
label
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
@ast
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
@en
prefLabel
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
@ast
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution.
@en
P2093
P356
P1433
P1476
Arsenic(III)-cysteine interactions stabilize three-helix bundles in aqueous solution
@en
P2093
B T Farrer
C P McClure
V L Pecoraro
P304
P356
10.1021/IC0010149
P407
P577
2000-11-01T00:00:00Z