Thermodynamic model for the stabilization of trigonal thiolato mercury(II) in designed three-stranded coiled coils.
about
Protein design: toward functional metalloenzymesStructural 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 metalloproteinA Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed MetalloproteinsDesigning hydrolytic zinc metalloenzymesControlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.Hg(II) binding to a weakly associated coiled coil nucleates an encoded metalloprotein fold: a kinetic analysis.Influence of active site location on catalytic activity in de novo-designed zinc metalloenzymes.Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy MetalsExperimental and theoretical evaluation of multisite cadmium(II) exchange in designed three-stranded coiled-coil peptidesDesigning a functional type 2 copper center that has nitrite reductase activity within α-helical coiled coilsThe 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 proteinsDesign of thiolate rich metal binding sites within a peptidic framework.Designing 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.De novo-designed metallopeptides with type 2 copper centers: modulation of reduction potentials and nitrite reductase activities.Heterochromia in designed metallopeptides: geometry-selective binding of CdII in a de novo peptide.Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site.De novo protein design as a methodology for synthetic bioinorganic chemistry.Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up.Incorporation of second coordination sphere D-amino acids alters Cd(II) geometries in designed thiolate-rich proteins.Modifying the Sterics In the Second Coordination Sphere Of Designed Peptides Leads to Enhancement of Nitrite Reductase Activity.Sculpting Metal-binding Environments in De Novo Designed Three-helix Bundles.Lead(II) Binding in Natural and Artificial Proteins.Cyclic Phosphopeptides to Rationalize the Role of Phosphoamino Acids in Uranyl Binding to Biological Targets.Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To GoClarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein
P2860
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P2860
Thermodynamic model for the stabilization of trigonal thiolato mercury(II) in designed three-stranded coiled coils.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Thermodynamic model for the stabilization of trigonal thiolato mercury
@nl
Thermodynamic model for the st ...... d three-stranded coiled coils.
@en
type
label
Thermodynamic model for the stabilization of trigonal thiolato mercury
@nl
Thermodynamic model for the st ...... d three-stranded coiled coils.
@en
prefLabel
Thermodynamic model for the stabilization of trigonal thiolato mercury
@nl
Thermodynamic model for the st ...... d three-stranded coiled coils.
@en
P2093
P356
P1433
P1476
Thermodynamic model for the st ...... d three-stranded coiled coils.
@en
P2093
Balchus KE
Pecoraro VL
P304
14696-14705
P356
10.1021/BI015649A
P407
P577
2001-12-01T00:00:00Z