The TMCrys server for supporting crystallization of transmembrane proteins

Bioinformatics
Julia K Varga, Gábor E Tusnády

Abstract

Due to their special properties, the structures of transmembrane proteins are extremely hard to determine. Several methods exist to predict the propensity of successful completion of the structure determination process. However, available predictors incorporate data of any kind of proteins, hence they can hardly differentiate between crystallizable and non-crystallizable membrane proteins. We implemented a web server to simplify running TMCrys prediction method that was developed specifically to separate crystallizable and non-crystallizable membrane proteins. http://tmcrys.enzim.ttk.mta.hu. Supplementary data are available at Bioinformatics online.

References

Sep 5, 2002·Nature Reviews. Drug Discovery·Andrew L Hopkins, Colin R Groom
May 8, 2004·Bioinformatics·Li ChenJohn Westbrook
Dec 31, 2005·Nucleic Acids Research·Andrei KouranovHelen M Berman
Jul 1, 2006·FEBS Letters·Ian M Overton, Geoffrey J Barton
Sep 19, 2007·Proteins·Antonio J Martin-GalianoDmitrij Frishman
Nov 18, 2008·Nucleic Acids Research·Helen M BermanJoshua La Baer
Aug 4, 2009·BMC Structural Biology·Bent PetersenClaus Lundegaard
Dec 4, 2012·Nucleic Acids Research·Dániel KozmaGábor E Tusnády
May 29, 2015·Biology Direct·László DobsonGábor E Tusnády
Dec 8, 2016·Nucleic Acids Research·Julia VargaGábor E Tusnády
May 3, 2018·Bioinformatics·Julia K Varga, Gábor E Tusnády

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Software Mentioned

PepcDB
Apache Axis
Laravel
TMCrys
XGBoost
Bootstrap
TargetDB
TargetTrack
CCTOP

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