The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes-Reference-Cited by-同舟云学术

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The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes

Published:1991-01 Issue:1 Volume:10 Page:50-69
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Noble Martin E. M.,Wierenga Rik K.,Lambeir Anne-Marie,Opperdoes Fred R.,Thunnissen Andy-Mark W. H.,Kalk Kor H.,Groendijk Hillie,Hol Wim G. J.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference45 articles.

1. Perfection in enzyme catalysis: the energetics of triosephosphate isomerase

2. Free-energy profile for the reaction catalyzed by triosephosphate isomerase

3. The Mechanism of the Triosephosphate Isomerase Reaction

4. Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy

5. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

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2. Conformational dynamics of active site loops 5, 6 and 7 of enzyme Triosephosphate Isomerase: A molecular dynamics study;2018-11-03

3. The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases—Part III: In-Silico Molecular Docking Investigations;Molecules;2016-10-19

4. Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency;Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease;2015-01

5. BP-Dock: A Flexible Docking Scheme for Exploring Protein–Ligand Interactions Based on Unbound Structures;Journal of Chemical Information and Modeling;2014-03-04

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