World Library  


Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos Computational Biology : Probing the Mutational Interplay Between Primary and Promiscuous Protein Functions ; a Computational Experimental Approach, Volume 8

By Garcia-seisdedos, Hector

Click here to view

Book Id: WPLBN0003941374
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos Computational Biology : Probing the Mutational Interplay Between Primary and Promiscuous Protein Functions ; a Computational Experimental Approach, Volume 8  
Author: Garcia-seisdedos, Hector
Volume: Volume 8
Language: English
Subject: Journals, Science, Computational Biology
Collections: Periodicals: Journal and Magazine Collection (Contemporary), PLoS Computational Biology
Historic
Publication Date:
Publisher: Plos

Citation

APA MLA Chicago

Garcia-Seisdedos, H. (n.d.). Plos Computational Biology : Probing the Mutational Interplay Between Primary and Promiscuous Protein Functions ; a Computational Experimental Approach, Volume 8. Retrieved from http://ebook.worldlibrary.net/


Description
Description : Description:Protein promiscuity is of considerable interest due its role in adaptive metabolic plasticity, its fundamental connection with molecular evolution and also because of its biotechnological applications. Current views on the relation between primary and promiscuous protein activities stem largely from laboratory evolution experiments aimed at increasing promiscuous activity levels. Here, on the other hand, we attempt to assess the main features of the simultaneous modulation of the primary and promiscuous functions during the course of natural evolution. The computational/experimental approach we propose for this task involves the following steps : a function-targeted, statistical coupling analysis of evolutionary data is used to determine a set of positions likely linked to the recruitment of a promiscuous activity for a new function: a combinatorial library of mutations on this set of positions is prepared and screened for both, the primary and the promiscuous activities: a partial-least-squares reconstruction of the full combinatorial space is carried out: finally, an approximation to the Pareto set of variants with optimal primary/promiscuous activities is derived. Application of the approach to the emergence of folding catalysis in thioredoxin scaffolds reveals an unanticipated scenario : diverse patterns of primary/promiscuous activity modulation are possible, including a moderate (but likely significant in a biological context) simultaneous enhancement of both activities. We show that this scenario can be most simply explained on the basis of the conformational diversity hypothesis, although alternative interpretations cannot be ruled out. Overall, the results reported may help clarify the mechanisms of the evolution of new functions. From a different viewpoint, the partial-least-squaresreconstruction/ Pareto-set-prediction approach we have introduced provides the computational basis for an efficient directed-evolution protocol aimed at the simultaneous enhancement of several protein features and should therefore open new possibilities in the engineering of multi-functional enzymes

 

Click To View

Additional Books


  • Plos Computational Biology : Refining Pr... (by )
  • Plos Computational Biology : Analysis of... (by )
  • Plos Computational Biology : Modeling Ne... (by )
  • Plos Computational Biology : a Threading... (by )
  • Plos Computational Biology : Dynamic Mod... (by )
  • Plos Computational Biology : Context-dep... (by )
  • Plos Computational Biology : Quantitativ... (by )
  • Plos Computational Biology : Tuning Prom... (by )
  • Plos Computational Biology : Timing the ... (by )
  • Plos Computational Biology : Efficient S... (by )
  • Plos Computational Biology : Intrinsic D... (by )
  • Plos Computational Biology : Effects of ... (by )
Scroll Left
Scroll Right

 



Copyright © World Library Foundation. All rights reserved. eBooks from World eBook Library 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.