S. Durani

    Professor

    Department of Chemistry

    Indian Institute of Technology Bombay

    Powai, Mumbai 400076

    Ph:   022-2576 7164

    Fax:  022-2576 3480

    Email: sdurani[at]chem.iitb.ac.in

    Group Webpage

Academic Background

Graduation: Chemistry; 1970; Jammu University.

Master: Organic Chemistry; 1972; Jammu University.

Doctorate: Chemistry; 1977; Jammu University.

Professional Experience

1977-1982 Scientist B, CDRI, Lucknow.

1982 -1985 Scientist C, CDRI, Lucknow

1985-1987 Asst. Prof., IIT Bombay.

1987-1989 Assoc. Prof., IIT Bombay.

1989- Professor, IIT Bombay.

 

Research Interests

 

Areas of Interest: Bio-Organic Chemistry; Peptide and Protein Chemistry; Protein Folding Problem; De Novo Peptide and Protein Motif Design; Molecular Enzymology; Enzyme Mechanisms; Enzyme Inhibitor Design.
   

Objectives: To analyze structure-conformation and conformation-function relationship in peptides and proteins; To design peptido-mimetics and enzyme inhibitors for possible application as drugs; To analyze strategies for rational design of miniproteins and enzymes.
  

Contributions: Dr. Durani did his doctoral research at Central Drug Research Institute (CDRI), Lucknow, during 1972-77, with Dr. Nityanand, the then director of CDRI as his supervisor. He worked in field of Medicinal Chemistry and subject of Drug Discovery. Dr. Durani joined CDRI as a scientist in 1977 and continued in this position up to 1985. Leading a group of researchers Dr. Durani contributed in classifying Structure Activity Relationships in antiestrogens and accomplished rational design of a new antiestrogen as a potential drug for contraception , breast cancer and osteoporosis. He joined IIT Bombay in 1985 and is currently a Professor in Chemistry. He was instrumental in founding the Biotechnology Centre at IIT Bombay and was its Head during the period 1992-2002. At IIT Bombay he had worked on the broad field of Bio-Organic Chemistry. He has made contributions on subjects of enzyme action, protein folding and de novo design.

 

 

Representative Publications

  • Homochiral Stereochemistry: The Missing Link of Structure to Energetics in Protein Folding. Kumar, A.; Ramakrishnan, V; Ranbhor, R.; Patel, K;
    Durani, S. Journal of Physical Chemistry B 113, 51, 16435-16442, (2009)

  • Electrostatics-defying interaction between arginine termini as a thermodynamic driving force in protein-protein interaction. Pednekar, D.; Tendulkar, A.;
    Durani, S. PROTEINS: Structure, Function, and Bioinformatics 74, 1, 155-163 (2009)

  • Protein Design in L and D - Amino Acid Structures as the Alphabet. Durani, S. Accounts of Chemical Research 41,10, 1301-1308 (2008)

  • Analysis of Structural Consensus of the Zinc Coordination Centers of Metalloprotein Structures. Patel, K.; Kumar, A.; Durani, S. Biochimica et Biophysica
    Acta
    1774, 1247 1253 (2007)

  • A mixed-miniprotein stereochemically reprogrammed to high-binding affinity for acetylcholine. Rana, S.; Kundu, B.; Durani, S. Biopolymers 87, 4, 231-243
    (2007)

  • A double catgrip mixed and mini protein only 20 residues long. Rana, S.; Kundu, B.; Durani, S. Bioorg. Med. Chem. 15, 3874-3882 (2007)

  • The interplay of sequence and stereochemistry in defining conformation in proteins and polypeptides. Ranbhor,R.; Ramakrishnan,V.; Kumar,A.; Durani, S.
    Biopolymers83, 537-45 (2006)

  • The link between sequence and conformation in protein structures appears to be stereochemically established. Ramakrishnan, V.; Ranbhor, R.; Kumar, A.;
    Durani, S. Journal of Physical Chemistry B110,9314-9323, (2006)

  • Computational design of proteins stereochemically optimized in size, stability and folding speed. Joshi, S.; Rana, S.; Wangikar, P.; Durani,S. Biopolymers
    83,122-134 (2006)

  • A Small Peptide Stereochemically Customized as a Globular Fold with a Molecular Cleft. Rana, S.; Kundu, B.; Durani, S. Chem. Comm., 207-209 (2005).

  • Simulated Folding of Polypeptides of Diversified Molecular Tacticity.  Implication for Protein Folding and De novo Design. Ramakrishnan, V.;  Ranbhor, R.;
    Durani, S., Biopolymers, 78, 96-105 (2005).

  • Stereospecific Peptide Folds.  A Rationally Designed Molecular Bracelet. Rana, S.; Kundu, B.; Durani, S. Chem. Comm., 2462-2463 (2004).

  • Existence of Specific Folds in Polyproline-II Ensembles of an Unfolded alanine Peptide Detected by Molecular Dynamics. Ramakrishnan, V.; Ranbhor, R.;
    Durani, S., Journal of American Chemical Society.  126,16332-16333 (2004).

  • Mechanism-based protein design: Attempted "nucleation-condensation" approach to a possible minimal helix-bundle protein. Mohanraja, K.;
    Dhanasekaran, M.; Kundu, B.; Durani, S.. Department of Chemistry,  Indian Institute of Technology, Bombay,  Mumbai,  India. Biopolymers ,70(3),
    355-363,
    (2003).

  • Combined sequence and structure analysis of the fungal laccase family. Kumar, S. V. Suresh; Phale, Prashant S.; Durani, S.; Wangikar, Pramod P.
    Biotechnology and Bioengineering,  83(4),  386-394,
    (2003).

  • Solution conformation of a rationally designed nonapeptide. Dhanasekaran, M.; Srivastava, Sudha; Raju, E. B.; Durani, S. Physiological Chemistry and
    Physics and Medical NMR
      ,  33(2),  163-174, (2001).

  • Conformational effects of C -dipropargylglycine as a constrained residue. Damodharan, L.; Mohanraja, K.; Kotha, S.; Durani, S.; Pattabhi, V. Biopolymers
    59(5),  330-338, (2001).

  • Modification of constrained peptides by ring-closing metathesis reaction. Kotha, S.; Sreenivasachary, N.; Mohanraja, K.; Durani, S. Bioorganic &
    Medicinal Chemistry Letters
       11(11),  1421-1423,
    (2001).

  • Conformational preferences of heterochiral peptides. Crystal structures of heterochiral peptides Boc-(D) Val-(D) Ala-Leu-Ala-OMe and
    Boc-Val-Ala-Leu-(D) Ala-OMe- enhanced stability of -sheet through C-H...O hydrogen bonds. Fabiola, G. Felcy; Bobde, Vivek; Damodharan, L.;
    Pattabhil, Vasantha; Durani, S. Journal of Biomolecular Structure & Dynamics ,  18(4),  579-594, (2001).

  • N-1 and N-2 positional effects in the propagation of 310-type fold in the helical model peptide Boc-(D)Glu-Pro-Ala-Lys-Ala-Leu-Ala-OMe. Beri,S.;
    Srivastava, Sudha; Dhanasekaran, M.; Phadke, Ratna S.; Durani, S. Magnetic Resonance in Chemistry  38(4), 257-264,
    (2000).

  • A Rationally Designed Turn-Helix Peptide. Dhanasekaran, M.; Fabiola, F.; Pattabhi, V.; Durani, S. Journal of the American Chemical Society 121(23),
      5575-5576,
    (1999).