bjd12 at cus.cam.ac.uk
Tue May 11 04:07:04 EST 1993
Does anyone know if a Lys in close proximity to a Trp can cause
I've got a lysine lying along the indole ring of the
trp (the only one in the protein), with the NH3+ close to the
indole NH. When I unfold the protein, I see a large increase in
fluoresence as well as a redshift; the redshift I can understand,
the increase in fluoresence is the opposite to normal. There's no
other aromatics within 10A, and the trp is not solvent exposed.The lys
is part of a salt bridge with a glu and an asp.
Any suggestions ?
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