Thermal Unfolding of Triosephosphate Isomerase from Entamoeba histolytica: Dimer Dissociation Leads to Extensive Unfolding-Reference-Cited by-同舟云学术

Thermal Unfolding of Triosephosphate Isomerase from Entamoeba histolytica: Dimer Dissociation Leads to Extensive Unfolding

Published:2008-10-07 Issue:44 Volume:47 Page:11665-11673
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Tellez Luis A.¹,Blancas-Mejia Luis M.¹,Carrillo-Nava Ernesto¹,Mendoza-Hernández Guillermo¹,Cisneros David A.¹,Fernández-Velasco D. Alejandro¹

Affiliation:

1. Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, and Departamento de Fisicoquímica, Facultad de Química, Universidad Nacional Autónoma de México, Apdo. Postal 70-159, 04510 México, DF

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801360k

Reference49 articles.

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

2. Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase

3. The crystal structure of triosephosphate isomerase (TIM) fromThermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures

4. Three hTIM Mutants that Provide New Insights on why TIM is a Dimer

5. Kinetics and Energetics of Subunit Dissociation/Unfolding of TIM: The Importance of Oligomerization for Conformational Persistence and Chemical Stability of Proteins

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