Hi Pascal, Your problem brings to mind this paper:
FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties Science 3 November 2006: 314 (5800), 815-817.[DOI: 10.1126/science.1132516] Of course, in that case, the gellation was deliberate, but perhaps still worth a look. Cheers, Shane Caldwell McGill University On Mon, Apr 22, 2013 at 8:20 PM, Pascal Egea <pas...@msg.ucsf.edu> wrote: > Thanks to All for the diligent answers to my query, > > The protein is not thermophilic and has only one cysteine. We are working > in presence of freshly added reducing agent and glycerol to promote > solubility (well kinda it seems). > This is not an RNA or DNA binding protein and it has no low-complexity > regions except at the N terminus, there maybe some left over from a cryptic > transit peptide (somehow basic) that supposedly targets the protein to a > specific organelle. We are probably going to truncate further to see if it > solves our problem > > I appreciate all the comments and suggestions, > Cheers, > > Pascal > > -- > Pascal F. Egea, PhD > Assistant Professor > UCLA, David Geffen School of Medicine > Department of Biological Chemistry > Boyer Hall room 356 > 611 Charles E Young Drive East > Los Angeles CA 90095 > office (310)-983-3515 > lab (310)-983-3516 > email pe...@mednet.ucla.edu >
