World Library  


Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos One : Biophysical Characterization of the Dimer and Tetramer Interface Interactions of the Human Cytosolic Malic Enzyme, Volume 7

By Uversky, Vladimir, N.

Click here to view

Book Id: WPLBN0003934457
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos One : Biophysical Characterization of the Dimer and Tetramer Interface Interactions of the Human Cytosolic Malic Enzyme, Volume 7  
Author: Uversky, Vladimir, N.
Volume: Volume 7
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
Publication Date:
Publisher: Plos

Citation

APA MLA Chicago

Uversky, V. N. (n.d.). Plos One : Biophysical Characterization of the Dimer and Tetramer Interface Interactions of the Human Cytosolic Malic Enzyme, Volume 7. Retrieved from http://worldebookfair.com/


Description
Description : The cytosolic NADP+-dependent malic enzyme (c-NADP-ME) has a dimer-dimer quaternary structure in which the dimer interface associates more tightly than the tetramer interface. In this study, the urea-induced unfolding process of the c- NADP-ME interface mutants was monitored using fluorescence and circular dichroism spectroscopy, analytical ultracentrifugation and enzyme activities. Here, we demonstrate the differential protein stability between dimer and tetramer interface interactions of human c-NADP-ME. Our data clearly demonstrate that the protein stability of c-NADP-ME is affected predominantly by disruptions at the dimer interface rather than at the tetramer interface. First, during thermal stability experiments, the melting temperatures of the wild-type and tetramer interface mutants are 8–10uC higher than those of the dimer interface mutants. Second, during urea denaturation experiments, the thermodynamic parameters of the wild-type and tetramer interface mutants are almost identical. However, for the dimer interface mutants, the first transition of the urea unfolding curves shift towards a lower urea concentration, and the unfolding intermediate exist at a lower urea concentration. Third, for tetrameric WT c-NADP-ME, the enzyme is first dissociated from a tetramer to dimers before the 2 M urea treatment, and the dimers then dissociated into monomers before the 2.5 M urea treatment. With a dimeric tetramer interface mutant (H142A/D568A), the dimer completely dissociated into monomers after a 2.5 M urea treatment, while for a dimeric dimer interface mutant (H51A/D90A), the dimer completely dissociated into monomers after a 1.5 M urea treatment, indicating that the interactions of c-NADP-ME at the dimer interface are truly stronger than at the tetramer interface. Thus, this study provides a reasonable explanation for why malic enzymes need to assemble as a dimer of dimers.

 

Click To View

Additional Books


  • Plos One : Serum Fucosylated Haptoglobin... (by )
  • Plos One : Low Genetic Diversity in Wide... (by )
  • Plos One : Phylogenetic Evidence That Tw... (by )
  • Plos One : Effects of Handedness on Visu... (by )
  • Plos One : Endophyte-mediated Effects on... (by )
  • Plos One : when Parasitoid Males Make De... (by )
  • Plos One : Binding of the 9-o-n-aryl, Vo... (by )
  • Plos One : Critical Transitions in Early... (by )
  • Plos One : from Data Towards Knowledge ;... (by )
  • Plos One : Mdm2 Snp309 Rs2279744 Polymor... (by )
  • Plos One : Elucidation of Mirnas-mediate... (by )
  • Plos One : the Connectedness of Packed C... (by )
Scroll Left
Scroll Right

 



Copyright © World Library Foundation. All rights reserved. eBooks from World eBook Fair are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.