Advanced.Interfaces.Group
Research (Thesis Abstract)
Low-complexity regions appear to be common in protein sequences and although functions remain to be elucidated for most of them, they have been increasingly found to play crucial biological roles. Because most of these regions show poor conservation across protein families, it is difficult to compare them using common sequence analysis techniques.
This study asks whether low-complexity regions play important roles in protein binding and if they are crucial to the overall functions of the proteins to which they belong.
First, a methodology for detecting low-complexity regions in protein sequences was implemented; second, a database and bioinformatics tools, to query and visualise the results, were designed, implemented and released; finally, the developed framework was used to characterise the detected low-complexity regions.
Results, obtained from protein-protein interaction and gene ontology annotation analyses show evidence that low-complexity regions — and especially the ones situated at the terminal regions of their corresponding protein sequences — have strong binding capabilities. These binding capabilities, necessary to protein-complex formation, and their annotation enrichment in particular gene ontology terms, suggest low-complexity regions could play crucial roles in particular protein functions.
Matrices
leveinshtein_QC_42 entropy_QC_42 SW_QC_42
leveinshtein_YP_168 entropy_YP_168 SW_YP_168
leveinshtein_YF_30 entropy_YF_30 SW_YF_30
leveinshtein_K_100 entropy_K_100 SW_K_100
leveinshtein_K_1000 entropy_K_1000 SW_K_1000
leveinshtein_SPP_443 entropy_SPP_443 SW_SPP_443
leveinshtein_SPP_100 entropy_SPP_100 SW_SPP_100
Supervisors
Terri Attwood and Steve pettifer
Contact
alain.coletta@postgrad.manchester.ac.uk
tel +44 161 275 57 37
Michael Smith Building, B.1079
School of biological sciences,
University of Manchester M13 9PT
Manchester UK