Y. U. Sasidhar

    Professor

    Department of Chemistry

    Indian Institute of Technology Bombay

    Powai, Mumbai 400076

    Ph:   022-2576 7179

    Fax:  022-2576 7152

    Email: sasidhar[at]chem.iitb.ac.in

    Group Webpage

Academic Background

M. Sc. Indian Institute of Technology Madras, Chennai 600 036

Ph. D. Indian Institute of Technology Madras, Chennai 600 036

Professional Experience

Visiting Fellow,Chemical Physics Group ,Tata Institute of Fundamental Research (TIFR), 1986-1989

Associate Professor, Indian Institute of Technology Bombay 1989-

 

Research Interests

  • Biophysical Chemistry  (General)

  • Probing protein folding and protein dynamics with molecular dynamics simulations. (specific)

Representative Publications

 

Patel, S., Sasidhar, Y.U. (2008) A shorter peptide model from staphylococcal nuclease for the folding-unfolding equilibrium of a beta-hairpin shows that unfolded state has significant contribution from compact conformational states . J Struct Biol. 2008 Oct;164(1):60-74.

Patel, S., Taimni R., Sasidhar, Y.U. (2007) A small tripeptide AFA undergoes two state cooperative conformational transitions: Implications for conformational biases in unfolded states. Protein Pept. Lett. 14:581-9.

Sujatha, M.S., Sasidhar,Y.U.  and Balaji, P.V., (2007) MP2/6-311++G(d,p) study on galactose-aromatic residue analog complexes in different position-orientations of the saccharide relative to aromatic residues. J. Mol. Struct. (Theochem),.814, 11-24.

Patel, S., Balaji, P.V., Sasidhar, Y.U. (2007) The sequence TGAAKAVALVL from glyceraldehyde-3-phosphate dehydrogenase displays structural ambivalence and interconverts between alpha-helical and beta-hairpin conformations mediated by collapsed conformational states. J. Pept. Sci., 13, 314-26.

Patel, S., Sista, P., Balaji, P.V., Sasidhar, Y.U. (2006) Beta-hairpins with native-like and non-native hydrogen bonding patterns could form during the refolding of staphylococcal nuclease. J. Mol. Graph. Model., 25,103-15.

M.S.Sujatha, Sasidhar,Y.U. and Balaji, P.V. (2005) Insights into the role of aromatic residue in galactose-binding sites: MP2/6-311G++** study on galactose- and glucose-aromatic residue analog complexes. Biochemistry, 44, 8554-8562. 


M.S.Sujatha, Sasidhar,Y.U. and Balaji, P.V. (2004) Energetics of galactose- and glucose-aromatic amino acid interactions: implications for binding in galactose-specific proteins. Protein Sci., 13, 2502-2514.

Sasidhar, Y. U.  and Ratna Prabha, C. (2000) Conformational features of reduced and disulfide intact forms  of hen egg white lysozyme   in   aqueous   solution   in    the    presence    of 3-chloro-1,2-propanediol and  dioxane  :  Implications  for protein folding intermediates. Indian J. Biochem. Biophys., 37, 97-106.
 
Sasidhar, Y. U. and Ramakrishna, V. (2000) Conformational features of a hexapeptide model Ac-TGAAKA-NH2 corresponding to a hydrated a helical segment from Glyceraldehyde 3-Phosphate  Dehydrogenase : Implications for the role of turns in helix folding. Indian J. Biochem. Biophys., 37, 34-44.

Sasidhar, Y. U., Ratna Prabha, C. and Gidwani, A. (1999) Conformational features of certain peptides from lysozyme and their possible role in the folding of lysozyme. Journal of Biosciences, 24, Supplement 1, 64.

Ratnaprabha, C. and Sasidhar, Y. U. (1998) Conformational features of disulfide intact and reduced forms of hen egg white lysozyme in aqueous solution in the presence of  trifluoroethanol (TFE): Implications for protein folding intermediates. J. Chem. Soc., Faraday Trans., 94, 3631-3637.

Ramakrishna, V. and Sasidhar, Y. U. (1998 ) Conformational features of a peptide model Ac-DTVKLMYKGQPMTFR-NH2, corresponding to  an early folding b hairpin region of Staphylococcal  nuclease. Indian J. Biochem. Biophys., 35, 333- 338. 

Ramakrishna, V.  and Sasidhar, Y. U. (1997) A Pentapeptide Model for an Early Folding Step in the Refolding of Staphylococcal Nuclease : The Role of its Turn Propensity. Biopolymers, 41, 181-191.