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: vnambood...@locuspharma.com Ph: 215-358-2012 Fax: 215-358-2020
