Document Detail


Disorderness in Escherichia coli proteome: perception of folding fidelity and protein-protein interactions.
MedLine Citation:
PMID:  22889400     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Traditionally biased usage of synonymous codons renders selective advantage to proteins expressed at high levels with a few exceptions like in Escherichia coli. Proteome-wide characteristics indicative of trends in highly expressed proteins of E. coli is analyzed in this communication. Implications for the nature of interactions performed by these two groups of highly expressed proteins are discussed here. The group of highly expressed proteins having optimized codon usage through employment of most abundant tRNAs is already shielded from misfolding by their improved error-prone translational machinery. Our data also provide evidence for mechanism by which a significant proportion of highly expressed proteins with high intrinsic disorder evade degradation and successfully carry out their function.
Authors:
Bratati Kahali; Tapash Chandra Ghosh
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-8-13
Journal Detail:
Title:  Journal of biomolecular structure & dynamics     Volume:  -     ISSN:  1538-0254     ISO Abbreviation:  J. Biomol. Struct. Dyn.     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-8-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8404176     Medline TA:  J Biomol Struct Dyn     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
a Bioinformatics Centre, Bose Institute , P 1/12, C.I.T. Scheme VII M , Kolkata , 700 054 , India.
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