Hello
I am designing a protein construct for structural biology. It is a protein kinase
which has not been crystallized earlier. I was comparing the kinase domains of
other closely related family members characterized biochemically vs
crystallization constructs. For crystallography constructs, there are different
stretches of amino acid residues particularly at the N-terminus (some contain
extra 2-5 residues while others have 15-20 residues.
My question: Is there a rational way of designing exact constructs one
would propose to make, eg., by a sequence alignment showing nearest
homology neighbors that guided construct design etc..
Sincerely
Hari
Haridasan V. M. Namboodiri, PhD
Scientist-Structural Biology
Locus Pharmaceuticals, Inc.
Four Valley Square
512 Township Line Road
Blue Bell, PA 19422
email: [log in to unmask]
Ph: 215-358-2012
Fax: 215-358-2020
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