Protein Bioinformatics Research Group

Disordered regions in transmembrane proteiins

Structurally transmembrane proteins are highly ordered in the membrane-spanning regions, but may contain disordered regions in the cytosolic and extra-cytosolic parts. We are involved in investigatie these disordered regions in transmembrane proteins. We applied a stringent definition of disordered residues on the currently available largest experimental dataset, and a significant correlation was found between the spatial distributions of positively charged residues and disordered regions. This finding suggests a new role of disordered regions in transmembrane proteins by providing structural flexibility for stabilizing interactions with negatively charged head groups of the lipid molecules.

People working on this project

Gábor E. Tusnády
László Dobson

Collaborating partners

Péter Tompa
VIB Structural Biology Research Center

Related publications

1. Dobson, L, Mészáros, B and Tusnády, GE (2018) Structural Principles Governing Disease-Causing Germline Mutations. J Mol Biol 430: 4955-4970.
2. Tusnády, GE, Dobson, L and Tompa, P (2015) Disordered regions in transmembrane proteins. Biochim Biophys Acta 1848: 2839-48.
3. Dobson, L and Tusnády, GE (2021) MemDis: Predicting Disordered Regions in Transmembrane Proteins. Sci Rep 22: .

News

2020-06-02 - Paper published
2019-03-08 - PhD degree
2019-02-07 - Paper published
2018-11-14 - Scientific Students' Association third prize
2018-10-30 - Paper published