Origins of catalysis by computationally designed retroaldolase enzymes. - Wikidata - wikimedia - TriplyDB

Origins of catalysis by computationally designed retroaldolase enzymes.

Origins of catalysis by computationally designed retroaldolase enzymes.

http://www.wikidata.org/entity/Q33740304

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Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymes Beyond directed evolution--semi-rational protein engineering and design Engineering a model protein cavity to catalyze the Kemp elimination Structural Analyses of Covalent Enzyme–Substrate Analog Complexes Reveal Strengths and Limitations of De Novo Enzyme Design Evolution of a designed retro-aldolase leads to complete active site remodeling Small molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shifts A Promiscuous De Novo Retro-Aldolase Catalyzes Asymmetric Michael Additions via Schiff Base Intermediates Keep on moving: discovering and perturbing the conformational dynamics of enzymes Computational protein engineering: bridging the gap between rational design and laboratory evolution.Conformational diversity and computational enzyme design Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins.Bovine serum albumin-catalyzed deprotonation of [1-(13)C]glycolaldehyde: protein reactivity toward deprotonation of the alpha-hydroxy alpha-carbonyl carbon.Optimizing non-natural protein function with directed evolution.Four small puzzles that Rosetta doesn't solve.Computational tools for rational protein engineering of aldolases.Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site.Dissecting enzyme function with microfluidic-based deep mutational scanning Computational strategies for the design of new enzymatic functions The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme.A highly efficient cocaine-detoxifying enzyme obtained by computational design.Computational design of protein-ligand interfaces: potential in therapeutic development.Emerging themes in the computational design of novel enzymes and protein-protein interfaces.Computational enzyme design.Protein engineering for metabolic engineering: current and next-generation tools.Computational design gains momentum in enzyme catalysis engineering.Computational Enzyme Design: Advances, hurdles and possible ways forward Recent advances in rational approaches for enzyme engineering.Enzyme architecture: on the importance of being in a protein cage.Computational tools for the evaluation of laboratory-engineered biocatalysts.Catalytic diversity in self-propagating peptide assemblies.Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily Robust design and optimization of retroaldol enzymes.Design of an allosterically regulated retroaldolase.Computational design of a Diels-Alderase from a thermophilic esterase: the importance of dynamics.Systematic optimization model and algorithm for binding sequence selection in computational enzyme design.Aldolase activity of serum albumins.Role of Conformational Dynamics in the Evolution of Retro-Aldolase Activity.QM/MM Analysis of Transition States and Transition State Analogues in Metalloenzymes.Regulation and Plasticity of Catalysis in Enzymes: Insights from Analysis of Mechanochemical Coupling in Myosin.

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Origins of catalysis by computationally designed retroaldolase enzymes.

http://www.wikidata.org/entity/Q33740304

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Origins of catalysis by computationally designed retroaldolase enzymes.

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Origins of catalysis by computationally designed retroaldolase enzymes.

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Origins of catalysis by computationally designed retroaldolase enzymes.

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Origins of catalysis by computationally designed retroaldolase enzymes.

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Origins of catalysis by computationally designed retroaldolase enzymes.

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Origins of catalysis by computationally designed retroaldolase enzymes.

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PNAS.0913638107

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

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Origins of catalysis by computationally designed retroaldolase enzymes.

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P2093

Daniel Herschlag

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David Baker

http://www.w3.org/2001/XMLSchema#string

Jonathan K Lassila

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P2860

De novo computational design of retro-aldol enzymes

Kemp elimination catalysts by computational enzyme design

The origin of the electrostatic perturbation in acetoacetate decarboxylase

De novo protein design: fully automated sequence selection

Immune versus natural selection: antibody aldolases with enzymic rates but broader scope

Challenges in enzyme mechanism and energetics

PK of the lysine amino group at the active site of acetoacetate decarboxylase.

Potential energy functions for protein design.

Combinatorial methods for small-molecule placement in computational enzyme design.

Aldol sensors for the rapid generation of tunable fluorescence by antibody catalysis.

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4937-4942

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scholarly article

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10.1073/PNAS.0913638107

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107

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20194782

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2841948

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