BioSysBio:abstracts/2007/Sanne Abeln: Difference between revisions
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==Motivation== | ==Motivation== | ||
At present there is no universal understanding how proteins can change topology during evolution, and how such pathways can be determined in a systematic way. <!-- Previously several mechanisms for topology evolution have been proposed, inculding ....... --> | At present there is no universal understanding how proteins can change topology during evolution, and how such pathways can be determined in a systematic way. <!-- Previously several mechanisms for topology evolution have been proposed, inculding ....... --> | ||
Revision as of 05:53, 28 September 2006
Linking evolution of protein structures through fragments
Author(s): Sanne Abeln, Charlotte M. Deane
Affiliations: University of Oxford
Contact:email: abeln@stats.ox.ac.uk
Keywords: 'protein structure' 'evolution' 'fragments' 'completed genomes'
Summary
Here we use a strucutural fragment library to investigate evolutionary links between protein folds. We show that 'older' folds have relatively more such links than 'younger' folds.
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Motivation
At present there is no universal understanding how proteins can change topology during evolution, and how such pathways can be determined in a systematic way. The ability to create links between fold topologies would have important consequences for structural classification, structure prediction and homology modelling. It has been proven difficult however to show the evolutionary relevance of previously established geometric measures to create links between topologies. Here we use our a previously determined age measure for protein folds or superfamilies to investigate the effect of evolution.[1]
Results
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Materials/Methods
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Conclusion
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References
- ↑ How old is your fold, Winstanley et al.
