Extreme electric fields power catalysis in the active site of ketosteroid isomerase - Wikidata - awgldk - TriplyDB

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

http://www.wikidata.org/entity/Q34454777

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The Use of Multiscale Molecular Simulations in Understanding a Relationship between the Structure and Function of Biological Systems of the Brain: The Application to Monoamine Oxidase Enzymes Mitochondrial Dysfunction and Disturbed Coherence: Gate to Cancer.Molecular sled is an eleven-amino acid vehicle facilitating biochemical interactions via sliding components along DNA.Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole Perspective: Defining and quantifying the role of dynamics in enzyme catalysis Vibrational Stark Effects of Carbonyl Probes Applied to Reinterpret IR and Raman Data for Enzyme Inhibitors in Terms of Electric Fields at the Active Site Enhancing the Oxidation of Toluene with External Electric Fields: a Reactive Molecular Dynamics Study A Critical Test of the Electrostatic Contribution to Catalysis with Noncanonical Amino Acids in Ketosteroid Isomerase Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.Long- and Short-Range Electrostatic Fields in GFP Mutants: Implications for Spectral Tuning Dissecting Proton Delocalization in an Enzyme's Hydrogen Bond Network with Unnatural Amino Acids.Exploring the chemistry and evolution of the isomerases BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase"Regulation of protein-ligand binding affinity by hydrogen bond pairing.Arylfluorosulfates Inactivate Intracellular Lipid Binding Protein(s) through Chemoselective SuFEx Reaction with a Binding Site Tyr Residue Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site.Measuring electric fields and noncovalent interactions using the vibrational stark effect.Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology.Oriented electric fields as future smart reagents in chemistry.Minimalist IR and fluorescence probes of protein function.Electric Fields and Enzyme Catalysis.Energy parasites trigger oncogene mutation.Prediction of distal residue participation in enzyme catalysis.Quantum mechanical calculation of electric fields and vibrational Stark shifts at active site of human aldose reductase.Electric-field-driven electron-transfer in mixed-valence molecules.Mechanism and bottlenecks in strand photodissociation of split green fluorescent proteins (GFPs).BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".Quantified electrostatic preorganization in enzymes using the geometry of the electron charge density.Predictive methods for computational metalloenzyme redesign - a test case with carboxypeptidase A.BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".Rate turnover in mechano-catalytic coupling: A model and its microscopic origin.Difference FTIR Studies of Substrate Distribution in Triosephosphate Isomerase.Electrostatic catalysis of a Diels-Alder reaction.Solvent-Independent Anharmonicity for Carbonyl Oscillators.Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Predicting substituent effects on activation energy changes by static catalytic fields."Inverse Drug Discovery" Strategy To Identify Proteins That Are Targeted by Latent Electrophiles As Exemplified by Aryl Fluorosulfates.Electric Fields and Fast Protein Dynamics in Enzymes.Correlating the vibrational spectra of structurally related molecules: A spectroscopic measure of similarity.

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P2860

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

http://www.wikidata.org/entity/Q34454777

description

2014 nî lūn-bûn

@nan

2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

@zh-hk

2014年論文

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2014年論文

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2014年论文

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name

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

@ast

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

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Extreme electric fields power catalysis in the active site of ketosteroid isomerase

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type

label

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

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Extreme electric fields power catalysis in the active site of ketosteroid isomerase

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Extreme electric fields power catalysis in the active site of ketosteroid isomerase

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prefLabel

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

@ast

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

@en

Extreme electric fields power catalysis in the active site of ketosteroid isomerase

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SCIENCE.1259802

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Extreme electric fields power catalysis in the active site of ketosteroid isomerase

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P2093

Sayan Bagchi

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Stephen D Fried

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P2860

Testing electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion hole

A proficient enzyme

Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymes

Improved side-chain torsion potentials for the Amber ff99SB protein force field

Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect

Comparison of simple potential functions for simulating liquid water

Roles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B

Asp-99 donates a hydrogen bond not to Tyr-14 but to the steroid directly in the catalytic mechanism of Delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B

Pseudoreversion of the catalytic activity of Y14F by the additional substitution(s) of tyrosine with phenylalanine in the hydrogen bond network of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B

Maintenance of alpha-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B

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1510-1514

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scholarly article

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10.1126/SCIENCE.1259802

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6216

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346

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Steven G. Boxer

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2014-12-01T00:00:00Z

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269767694

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25525245

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4668018

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