Using diastereopeptides to control metal ion coordination in proteins
about
Protein design: toward functional metalloenzymesSwitching the Chirality of the Metal Environment Alters the Coordination Mode in Designed PeptidesStructural 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 MetalloproteinsControlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.Cadmium(II) complex formation with cysteine and penicillamined-Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils.Cadmium(II) N-acetylcysteine complex formation in aqueous solution.Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.Design of functional metalloproteins.Design of a three-helix bundle capable of binding heavy metals in a triscysteine environment.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 peptidesThe importance of stereochemically active lone pairs for influencing Pb(II) and As(III) protein bindingDirect Observation of Nanosecond Water Exchange Dynamics at a Protein Metal SiteThe correlation of 113Cd NMR and 111mCd PAC spectroscopies provides a powerful approach for the characterization of the structure of Cd(II)-substituted Zn(II) proteinsDesigning functional metalloproteins: from structural to catalytic metal sites.Methods for Solving Highly Symmetric De Novo Designed Metalloproteins: Crystallographic Examination of a Novel Three-Stranded Coiled-Coil Structure Containing d-Amino Acids.Variable primary coordination environments of Cd(II) binding to three helix bundles provide a pathway for rapid metal exchange.Nutritional and medicinal aspects of D-amino acids.De Novo Design of Xeno-Metallo Coiled Coils.De novo protein design as a methodology for synthetic bioinorganic chemistry.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.Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To Go
P2860
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P2860
Using diastereopeptides to control metal ion coordination in proteins
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Using diastereopeptides to control metal ion coordination in proteins
@en
type
label
Using diastereopeptides to control metal ion coordination in proteins
@en
prefLabel
Using diastereopeptides to control metal ion coordination in proteins
@en
P2093
P2860
P50
P356
P1476
Using diastereopeptides to control metal ion coordination in proteins
@en
P2093
Anna F A Peacock
Lars Hemmingsen
Vincent L Pecoraro
P2860
P304
16566-16571
P356
10.1073/PNAS.0806792105
P407
P577
2008-10-21T00:00:00Z