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Name: Dr. R. Mahalakshmi
Designation: Assistant Professor
Department: Biology
E-Mail: maha@iiserbhopal.ac.in
Phone: +91-755-4092318
Fax: +91-755-4092392
Academic Profile:
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Assistant Professor (June 2009 - Present), Biology, Indian Institute of Science Education and Research, Bhopal, India.
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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.
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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.
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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:
- Biochemical and biophysical characterization of membrane proteins under near-native conditions.
- Membrane protein structure determination using Nuclear Magnetic Resonance (NMR) and other spectroscopic methods.
- Structural studies of transmembrane and membrane-associated peptides in lipid environments.
Selected Publications:
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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.
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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”.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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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