Understanding the structural and functional properties of intrinsically disordered proteins and their involvement in various diseases. Current research goals are: modeling the thermodynamic basis of order and disorder in proteins; recognizing functional sites within disordered proteins; understanding the specific roles of protein disorder in cancer. Various theoretical and computational approaches are utilized including simplified biophysical models, bioinformatic prediction methods and system biology approaches.
Is there a biological cost of protein disorder? Analysis of cancer-associated mutations.
MOL BIOSYST 8: (1) 296-307, 2012
ANCHOR: web server for predicting protein binding regions in disordered proteins.
BIOINFORMATICS 25: (20) 2745-2746, 2009
Prediction of Protein Binding Region in Disordered Proteins.
PLOS COMPUT BIOL 5: (5) , 2009
Molecular principles of the interactions of disordered proteins.
J MOL BIOL 372: (2) 549-561, 2007
The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins.
J MOL BIOL 347: (4) 827-839, 2005
ANCHOR aims to predict binding regions in proteins that are disordered in isolation but can undergo a disorder-to-order transition upon binding to a structured protein partner. The approach is based on the energy estimation method and it uses a single amino acid sequence as an input.
IUPred predicts intrinsically disoredered/unstructured proteins and protein regions. Intrinsically unstructured / disordered proteins have no single well-defined tertiary structure in their native, functional state. The IUPred server recognizes such regions from the amino acid sequence based on the estimated pairwise energy content.