Mahmood Tavallaie

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The botulinum neurotoxin A C-terminal fragment (Hc), which mediates the binding of the toxin to neuronal cell surface receptors, comprises two subdomains, Hc-N (amino acids 873-1095) and Hc-C (amino acids 1096-1296). In order to define the minimal fragment of Hc carrying protective antigenic properties, Hc, Hc-N and Hc-C have been produced as recombinant(More)
Microbial desulfurization is potentially an alternative process to chemical desulfurization of fossil fuels and their refined products. The dibenzothiophene desulfurizing system of Rhodococcus erythropolis includes DszD which is an NADH-dependent FMN oxidoreductase with 192 residues that is responsible for supplying reducing equivalents in the form of FMNH2(More)
C-terminal fragment of the Botulinum neurotoxin A comprises two sub-domains including H(C)-N and H(C)-C. Here, the conformational change of H(C)-N was studied by spectroscopic techniques. The results indicated that the partially unfolded state forms during unfolding of H(C)-N. This finding may shed light on poorly--known features of the protein.
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