3D Structure prediction
The topology of transmembrane proteins can be predicted quite accurately from their amino acid sequences. Based on the results of the topology predictions we developed a method, called TMFoldWeb that aid the modeling of transmembrane domain structure. To achieve this, we used the predicted interactions between transmembrane helices and the differences in the folding of transmembrane regions of various transmembrane proteins (this is called „fold recognition”, or „threading”).
People working on this project
| Gábor E. Tusnády |
| László Dobson |
| Csongor Gerdán |
| András Zeke |
Related publications
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1.
Dobson, L, Szekeres, LI, Gerdán, C, Langó, T, Zeke, A and Tusnády, GE
(2023)
TmAlphaFold database: membrane localization and evaluation of AlphaFold2 predicted alpha-helical transmembrane protein structures.
Nucleic Acids Res
51:
D517-D522.
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|
2.
Kozma, D and Tusnády, GE
(2015)
TMFoldWeb: a web server for predicting transmembrane protein fold class.
Biol Direct
10:
54.
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|
3.
Kozma, D and Tusnády, GE
(2015)
TMFoldRec: a statistical potential-based transmembrane protein fold recognition tool.
BMC Bioinformatics
16:
201.
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Recent publications
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 |