Dear CCP Fo(r)lks,
I wonder if someone could help me about prediction servers or programs
or molecular dynamics I could use/run to compare the wild type protein
structure and a mutant (I do not have the structure for the mutant),
with/without substrate. The mutation (Asparagine to Aspartate) enhanced
the hydrolysis of cellulosic substrates, increased the protein thermal
stability, without affecting the protein fold. It would be interesting
if there is a way to see the structural differences in the atomic and
interatomic interactions determining the increased activity we have
observed.
I really appreciate your comments, help and opinions.
Cheers,
Mirella
--
Mirella Vivoli Vega, PhD
Senior Postdoctoral Fellow
Department of Experimental and Clinical Biomedical Sciences,
University of Florence,Viale Morgagni 50, 50134, Florence, Italy
email: mirella.viv...@unifi.it
"I do not want to believe, I want to know"[c. Sagan]
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