Zsuzsanna Dosztányi

Department of Biochemistry
Eötvös Loránd University

1117 Budapest, Pázmány Péter sétány 1/C

Email: dosztanyi@caesar.elte.hu

Research interests

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.

Selected publications

Pajkos M, Meszaros B, Simon I, Dosztanyi Z:
Is there a biological cost of protein disorder? Analysis of cancer-associated mutations.
MOL BIOSYST 8: (1) 296-307, 2012
Dosztanyi Z, Meszaros B, Simon I:
ANCHOR: web server for predicting protein binding regions in disordered proteins.
BIOINFORMATICS 25: (20) 2745-2746, 2009
Meszaros B, Simon I, Dosztanyi Z:
Prediction of Protein Binding Region in Disordered Proteins.
PLOS COMPUT BIOL 5: (5) , 2009
Meszaros B, Tompa P, Simon I, Dosztanyi Z:
Molecular principles of the interactions of disordered proteins.
J MOL BIOL 372: (2) 549-561, 2007
Dosztanyi Z, Csizmok V, Tompa P, Simon I:
The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins.
J MOL BIOL 347: (4) 827-839, 2005

Complete publication list

Web servers

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.