By C. A. Rogers, J. E. Jayne et. al. (editors)
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Extra info for Analytic Sets (London school 1978)
And Hensley, P. (1997) Experimental dissection of protein-protein interactions in solution. Adv. Mol. Cell. , 22A, 279–337. 17. Gerber, E. J. (2007) A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem. Biophys. Res. , 355, 751–757. 18. R. (1999) Minimization of recombinant human Flt3 ligand aggregation at the Tm plateau: a matter of thermal reversibility. Biochemistry, 38, 5241–5247. 19. , et al. (2012) ABRF-MIRG benchmark study: molecular interactions in a three component system.
The method is conducted at conditions where the protein is in the native form, and the objective is to gain information about the solubility of the native form. We conducted ammonium sulfate salting-out studies on the EGFR mono-Adnectins to help select the candidates with the most favorable solubility behavior. 8. Most of the candidates had similar solubility behavior, but one lead candidate in particular had much lower solubility. The rank-order of estimated solubilities obtained by this higher throughput method was in good agreement with solubility limits measured by centrifugal spin concentration (data not shown), although the most soluble molecules could not be fully characterized by the spin method due to a lack of sufficient amounts of the candidate molecules to reach their upper limit solubility values.
Many N-linked glycosylated proteins have been crystallized, suggesting that leaving the asparagine residue in the construct may be acceptable. In cases where this is not the case, the standard procedures are to mutate the asparagine residue of the motif to a glutamine or to express in a system that suppresses glycosylation . org). Many of the proteins of interest in biotherapeutics are cell-surface receptors, attached to the cell surface by one or more TM spanning helices. Crystallizing the exo-region in the presence of these TMs has so far proven intractable, so the general method is to remove the TM from the construct.