I am designing some controls for an LSPR experiment using BSA and another protein of comparable size. BSA is very "sticky" (hydrophobic regions, surface thiol, highly charged), and so we'd like to run the controls with another protein with preferably less stickiness (to gold-coated in alkanethiols). Glutamate dehydrogenase is used in protein standards and almost exactly the same mass as BSA. Actin isn't as massive, but I've been led to believe that muscle proteins are less likely to be sticky. Does anyone have any insights on these matters? Particularly, is there a reliable resource to look at hydrophobicity, surface charge and surface thiols given a protein of known structure?
It does seem that G-Actin has a surface thiol:
http://www.ncbi.nlm.nih.gov/pubmed/2317199
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