Protein-protein interactions

Steve Rodems smrodems at
Thu Mar 10 00:43:55 EST 1994

I've been doing gel shift experiments to analyze protein-DNA interactions
and I've been using a Tris-glycing buffer system.  It is my understanding
that tris-glycine is of higher ionic strength than other commonly used gel
shift buffers (eg., TAE, TE, 0.5x TBE) and that with this system you tend
NOT to detect weaker interactions.  My question is:  Using tris-glycine are
protein-protein interactions stable?  That is, say a DNA binding protein
binds DNA as a homodimer but another non-DNA binding protein can interact
with the DNA binding protein through protein-protein interactions.  Can one
detect the non-DNA binding protein as part of the complex using a
tris-glycing buffer system.

Does anyone have ideas as to what gel system and/or binding buffers (salt
conc's) needed to detect protein-protein interactions as well as
protein-DNA interactions?

Steve "Some day I will get the hell out of Wisconsin" Rodems

"Then I am here for the Lee family renioun ... shur-wajo-shur"

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