Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins - Wikidata - awgldk - TriplyDB

Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins

Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins

http://www.wikidata.org/entity/Q27622718

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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Protein design: toward functional metalloenzymes Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites Design of a minimal protein oligomerization domain by a structural approach Preorganization of molecular binding sites in designed diiron proteins De novo designed cyclic-peptide heme complexes Identifying important structural characteristics of arsenic resistance proteins by using designed three-stranded coiled coils Solution NMR Structure of a Designed Metalloprotein and Complementary Molecular Dynamics Refinement Control of Protein Oligomerization Symmetry by Metal Coordination: C 2 and C 3 Symmetrical Assemblies through Cu II and Ni II Coordination Controlled Protein Dimerization through Hybrid Coordination Motifs Porous protein frameworks with unsaturated metal centers in sterically encumbered coordination sites Structural Comparisons of Apo- and Metalated Three-Stranded Coiled Coils Clarify Metal Binding Determinants in Thiolate Containing Designed Peptides Proton and metal ion-dependent assembly of a model diiron protein Artificial Diiron Enzymes with a De Novo Designed Four-Helix Bundle Structure Engineering a zinc binding site into the de novo designed protein DS119 with a βαβ structure De novo design of helical bundles as models for understanding protein folding and function.On the origin and highly likely completeness of single-domain protein structures.Designing hydrolytic zinc metalloenzymes Computational approaches for rational design of proteins with novel functionalities Probing designability via a generalized model of helical bundle geometry Achievements and Challenges in Computational Protein Design.Designing artificial enzymes by intuition and computation Lanthanide-binding helix-turn-helix peptides: solution structure of a designed metallonuclease.Noncovalent self-assembly of a heterotetrameric diiron protein.Structural principles for computational and de novo design of 4Fe-4S metalloproteins.De novo backbone scaffolds for protein design.Controlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions.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.Design of functional metalloproteins.Cys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ.Miniaturized metalloproteins: application to iron-sulfur proteins.De novo design of a transmembrane Zn²⁺-transporting four-helix bundle.Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins.Design of thiolate rich metal binding sites within a peptidic framework.Designing functional metalloproteins: from structural to catalytic metal sites.Spectroscopic definition of the biferrous and biferric sites in de novo designed four-helix bundle DFsc peptides: implications for O2 reactivity of binuclear non-heme iron enzymes An artificial di-iron oxo-protein with phenol oxidase activity.

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P2860

Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins

http://www.wikidata.org/entity/Q27622718

description

2000 nî lūn-bûn

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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2000 թվականի հունիսին հրատարակված գիտական հոդված

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2000年の論文

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Retrostructural analysis of me ...... imal model for diiron proteins

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Retrostructural analysis of me ...... imal model for diiron proteins

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Proceedings of the National Academy of Sciences of the United States of America

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Retrostructural analysis of me ...... imal model for diiron proteins

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C M Summa

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L Randaccio

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V Pavone

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W F DeGrado

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P2860

Structure and function of the Escherichia coli ribonucleotide reductase protein R2

Improved methods for building protein models in electron density maps and the location of errors in these models

PROCHECK: a program to check the stereochemical quality of protein structures

Alternative metal-binding sites in rubrerythrin

Solution structure and dynamics of a de novo designed three-helix bundle protein

Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts

Structures of deoxy and oxy hemerythrin at 2.0 A resolution

Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A

Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution

Structure of a unique twofold symmetric haem-binding site

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Silvano Geremia

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