Document Detail

Evolution of bacterial ribosomal protein L1.
MedLine Citation:
PMID:  22450273     Owner:  NLM     Status:  In-Data-Review    
Search vectors composed of Gly, Ala, Arg, and Pro (GARP) residues retrieve 98% of each of the ribosomal proteins in prokaryotic species with no false hits. Different combinations of G, A, R and P and insertions differentiate each ribosomal protein from all others. Amino acids in two sequence positions separate Gram+ from Gram- bacteria. Specific residues separate proteins of cyanobacteria and chloroplasts from all other species. Structural information played an essential role in developing a GARP based technique to achieve perfect sequence alignment. It is possible to understand why GARP residues are 100% conserved in specific positions in families of proteins present in all species.
William L Duax; Robert Huether; David Dziak
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  International journal of bioinformatics research and applications     Volume:  8     ISSN:  1744-5485     ISO Abbreviation:  Int J Bioinform Res Appl     Publication Date:  2012  
Date Detail:
Created Date:  2012-03-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101253758     Medline TA:  Int J Bioinform Res Appl     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  99-111     Citation Subset:  IM    
Department of Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott St., Buffalo, NY 14203, USA.
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