Dr. Md. Sohail Akhtar
 
 

Scientist Gr IV
Molecular and Structural Biology Division

 
Educational Qualifications M.Sc. (Calicut) Ph.D (JNU)
E Mail mdsohailakhtar@yahoo.com
RESEARCH AREAS
 
Molecular Biophysics / Protein Folding
 
HONOURS & AWARDS
CSIR Young Scientist Award-2006
National Academy of Sciences, India, Young Scientist Award-2006
 
 
SELECTED PUBLICATIONS
 
Akhtar. Md. S. and Bhakuni V. (2007) Role of ionic interactions and linker in the domain interaction and modulation of functional activity of hyaluronate lyase. Biochem. Biophys. Res. Commun. In press
Akhtar. Md. S., Krishnan, MY. and Bhakuni V. (2006) Insight into the mechanism of action of hyaluronate lyase; role of C-terminal domain and Ca2+ in the functional regulation of enzyme. J. Biol. Chem., 281, 28336-28344
Mishra P., Akhtar, Md. S. and Bhakuni V. (2006) Unusual structural features of the bacteriophage-associated hyaluronate lyase (HylP2). J. Biol. Chem., 281, 7143-7150
Akhtar. Md. S. and Bhakuni. V. (2004) Streptococcus pneumoniae hyaluronate lyase: an overview. Current Science. 86, 285-295.
Akhtar. Md. S. and Bhakuni. V. (2003) Streptococcus pneumoniae hyaluronate lyase contains two non-cooperative independent folding/unfolding structural domains: characterization of functional domain and inhibitors of enzyme. J. Biol. Chem., 278, 25509-25516
Akhtar. Md. S. and Bhakuni. V. (2003) Alkaline treatment has contrasting effects on the structure of deglycosylated and glycosylated forms of glucose oxidase. Arch. Biochem. Biophys., 413, 221-228
Akhtar. Md. S., Ahmad, A. and Bhakuni. V. (2002) Divalent cation induced changes in structural properties of the dimeric enzyme glucose oxidase: Dual effect of dimer stabilization and dissociation with loss of cooperative interactions in enzyme monomer. Biochemistry, 41, 7142-7149
Akhtar. Md. S., Ahmad, A. and Bhakuni. V. (2002) Guanidinium chloride- and urea-induced unfolding of the dimeric enzyme glucose oxidase. Biochemistry, 41, 3819-3827.
Ahmad, A. Akhtar. Md. S., and Bhakuni. V. (2002) Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme. Biochemistry, 40, 1945-1955.