Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme - Test2 - elhamkhani - TriplyDB

Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme

Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme

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A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies.

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Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme

http://www.wikidata.org/entity/Q27703607

description

2016 nî lūn-bûn

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2016 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2016 թվականի ապրիլին հրատարակված գիտական հոդված

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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name

Connecting Active-Site Loop Co ...... ue 96 in the Plasmodial Enzyme

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Connecting Active-Site Loop Co ...... ue 96 in the Plasmodial Enzyme

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Connecting Active-Site Loop Co ...... ue 96 in the Plasmodial Enzyme

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Connecting Active-Site Loop Co ...... ue 96 in the Plasmodial Enzyme

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Hemalatha Balaram

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Mathur R N Murthy

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Moumita Samanta

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Niranjan V Joshi

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Padmanabhan Balaram

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Vidhi Pareek

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Genome sequence of the human malaria parasite Plasmodium falciparum

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The role of water in the catalytic efficiency of triosephosphate isomerase

Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics

Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.

Functional role of the conserved active site proline of triosephosphate isomerase

Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site

Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95

Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway

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620-9

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scholarly article

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10.1002/CBIC.201500532

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7

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17

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2016-04-01T00:00:00Z

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26762569

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