INDIAN INSTITUTE OF SCIENCE EDUCATION AND RESEARCH BHOPAL

 

Name: Dr. R. Mahalakshmi
Designation: Assistant Professor
Department: Biology
E-Mail: maha@iiserb.ac.in
Phone: +91-755-4092318
Fax: +91-755-4092392

Academic Profile:

  • Assistant Professor (June 2009 - Present), Biology, Indian Institute of Science Education and Research, Bhopal, India.

  • Post-doc. Aug 2008 - May 2009, Department of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, CA, USA, with Drs. Carl Ware and Dirk Zajonc.

  • Post-doc. Nov 2006 - July 2008, Department of Apoptosis and Cell Death Research, Burnham Institute for Medical Research, La Jolla, CA, USA, with Dr. Francesca M. Marassi.

  • Ph. D. Aug 2003 - Oct 2006, in Molecular Biophysics from Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India, with Prof. P. Balaram.

Awards and Fellowships:

  • Awarded Innovative Young Biotechnologist Award (IYBA) 2009 by the Department of Biotechnology, Govt. of India.
  • Awarded Ramalingaswami Fellowship for the year 2009-10 by the Department of Biotechnology, Govt. of India.

Research Interest:

Overview:
Our focus is in obtaining an in-depth understanding of the structure, function and regulation of biologically and pharmaceutically relevant proteins, especially those that belong to the transmembrane family. We are interested in molecules involved in ion transport, microbial survival against host defense and proteins of the human immune system implicated in immune signaling. Our interests also include understanding the factors that drive local and global folding, which will enable production of stable peptidomimetics targeted towards drug design.

Current Students:

Maurya Svetlana Rajkumar: Svetlana is interested in the complete structural and biochemical characterization of ion channels of the human mitochondrial outer membrane. Her focus is primarily towards deducing the folding mechanism of these proteins and the influence of lipids on their fold, function and stability using a combination of biophysical, spectroscopic and NMR methods.

Kamlesh Madhusudan Makwana: Kamlesh is involved in the total synthesis and complete structural characterization of peptides designed to adopt specific secondary and supersecondary structures. He is also interested in the design, synthesis and biochemical characterization of peptide mimetics and the development of small molecule gene regulators.

Deepti Chaturvedi: Deepti is working on the biochemical and biophysical characterization of outer membrane proteins from pathogenic bacteria, which are critical for the survival of these pathogens in the host and effective evasion of the host immune response. She is looking into the structure, fold and mode of interaction of these proteins with their potential binding partners from the host organism.

Other Projects:

1. Our interest also lies in the study of the structure and regulation of death receptors and the interaction of specific amino acids in lipid raft formation. We are also interested in examining the role of palmitoylation in domain localization of these receptors, using mutagenesis, chemical synthesis and structural analyses.

2. We are also carrying out an in silico analysis of the mycobacterial genome and proteome for the identification and structural characterization of potential drug targets. We are also actively working on a database analysis of factors that stabilize secondary structures in proteins towards the synthesis of novel folds in designed sequences.

Selected Publications:

  1. Plesniak, LA, Mahalakshmi, R, Rypien, C, Yang, Y, Racic, J, Marassi, FM. Expression, refolding, and initial structural characterization of the Y. pestis Ail outer membrane protein in lipids. Biochim. Biophys. Acta 2010/11, doi:10.1016/j.bbamem.2010. 09.017.

  2. Petrovic, AG, Polavarapu, PL, Mahalakshmi, R and Balaram, P. Characterization of folded conformations in a tetrapeptide containing two tryptophan residues by vibrational circular dichroism (p S76-S85). Chirality 2009, DOI: 10.1002/chir.20779.

  3. Mahalakshmi, R and Marassi, FM. Orientation of the E. coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-state NMR. Biochemistry 2008, 47: 6531-6538. Selected as “Hot Article”.

  4. Mahalakshmi, R, Franzin, CM, Choi, J and Marassi, FM. NMR structural studies of the bacterial outer membrane protein OmpX in oriented lipid bilayer membranes. Biochim. Biophys. Acta (Biomembranes) 2007, 1768: 3216-3224.

  5. Mahalakshmi, R, Sengupta, A, Raghothama, S, Shamala, N and Balaram, P. Tryptophan rich peptides: influence of indole rings on backbone conformation. Biopolymers (Peptide Sci.) 2007, 88: 36-54.

  6. Mahalakshmi, R and Balaram, P. The use of D-amino acids in peptide design (book chapter). In D-amino acids: A new frontier in amino acid and protein research, Eds: Konno R, Brüeckner H, d' Aniello A, Fisher GH, Fujii N, Homma H. Nova Science Pub.; 2006, Chap. 5.9: 415-430.

  7. Mahalakshmi, R, Raghothama, S and Balaram, P. NMR analysis of aromatic interactions in designed peptide beta-hairpins. J. Am. Chem. Soc. 2006, 128: 1125-1138.

  8. Mahalakshmi, R and Balaram, P. Non-protein amino acids in the design of secondary structure scaffolds. Protein Design: Methods and Applications, Eds: Guerois R, de la Paz ML, Methods Mol. Biol. 2006, 340: 71-94; Humana Press.

  9. Mahalakshmi, R, Shanmugam, G, Polavarapu, PL and Balaram, P. Circular dichroism of designed peptide helices and beta-hairpins: Analysis of Trp- and Tyr-rich peptides. ChemBioChem 2005, 6: 2152-2157.

  10. Mahalakshmi, R, Sengupta, A, Raghothama, S, Shamala, N and Balaram, P. Tryptophan containing peptide helices: interactions involving the indole side chain. J. Peptide Res. 2005, 66: 277-296.

  11. Sengupta, A, Mahalakshmi, R, Shamala, N and Balaram, P. Aromatic interactions in tryptophan-containing peptides: Crystal structures of model tryptophan peptides and phenylalanine analogs. J. Peptide Res. 2005, 65: 113-129.

  12. Padmashri, R, Chakrabarti, KS, Sahal, D, Mahalakshmi, R, Sarma, SP and Sikdar, SK. Functional characterization of the pentapeptide QYNAD on rNav1.2 channels and its NMR structure. Pflugers. Arch. - Eur. J. Physiol. 2004, 447: 895-907.

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