Hypothetical protein Conclusion: Difference between revisions

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Through the combination of evolutionary, structural and functional analysis the hypothetical putative sugar binding protein 2ob5 was found to be a part of the RbsD/FucU superfamily. Through the use of literature review it was further identified that our protein appeared to be more specifically a FucU protein that catalysis the anomeric change of alpha-purine-fucose into beta-purine-fucose. This identification of function has come through the use of bioinformtatic tools and in order to verify these findings further scientifc experiments should be undertaken on these specific proteins.  
A combination of evolutionary, structural and functional have identified hypothetical putative sugar binding protein 2ob5 to belong to the RbsD/FucU superfamily of proteins. Furthermore, through identification and comparison of active sites, key binding residues and conserved regions, it is suggested that 2ob5 is a fucose-binding protein of the FuCU family. It was found that the biological unit of 2ob5's close structural analogs - and potentially 2ob5 - is a decameric non-membrane-bound oligomer. Functional analyses suggest that 2ob5 may catalyse the anomeric change of alpha-purine-fucose to beta-purine-fucose. Limitations in the scope of literature available necessitated some assumptions, and these conclusions would benefit from  confirmatory laboratory studies.  
 


[[Hypothetical protein Abstract | Abstract ]] | [[Hypothetical protein Introduction | Introduction]] | [[Hypothetical protein Method| Method]] |  
[[Hypothetical protein Abstract | Abstract ]] | [[Hypothetical protein Introduction | Introduction]] | [[Hypothetical protein Method| Method]] |  

Latest revision as of 01:22, 16 June 2009

A combination of evolutionary, structural and functional have identified hypothetical putative sugar binding protein 2ob5 to belong to the RbsD/FucU superfamily of proteins. Furthermore, through identification and comparison of active sites, key binding residues and conserved regions, it is suggested that 2ob5 is a fucose-binding protein of the FuCU family. It was found that the biological unit of 2ob5's close structural analogs - and potentially 2ob5 - is a decameric non-membrane-bound oligomer. Functional analyses suggest that 2ob5 may catalyse the anomeric change of alpha-purine-fucose to beta-purine-fucose. Limitations in the scope of literature available necessitated some assumptions, and these conclusions would benefit from confirmatory laboratory studies.

Abstract | Introduction | Method | Results | Discussion | Conclusion | References


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