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Personal Details

Designation : Associate Professor Department : Biological Sciences E-Mail : maha@iiserb.ac.in Phone : +91 755 269 1423, 669 1423 Fax : +91 755 669 2392



ACADEMIC DETAILS AND AWARDS RECEIVED


  • 2015 Apr - Present : Wellcome Trust / DBT India Alliance Intermediate Fellow.

    2014 Sep - Present : Associate Professor, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.

    2014 : NASI Young Scientist Platinum Jubilee Award, The National Academy of Sciences.

    2014 - 2017 : Associate, Indian Academy of Sciences.

    2014 : INSA Medal for Young Scientists, Indian National Science Academy.

    2010 – 2015 : Innovative Young Biotechnologist Award (IYBA) from the Department of Biotechnology, Govt. of India.

    2010 - 2015 : Ramalingaswami Fellow.

    2009 - 2014 : Assistant Professor in the Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.

    2008 - 2009 : Postdoctoral Fellow in the Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, La Jolla, CA, U.S.A.

    2006 - 2008 : Postdoctoral Associate in the Department of Apoptosis and Cell Death Research, Sanford-Burnham Medical Research Institute (previously Burnham Institute for Medical Research), La Jolla, CA, U.S.A.

    2003 - 2006 : Ph. D. in Molecular Biophysics from the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India, under the guidance of Prof. P. Balaram.

Information for New Candidates


  • May 2016: We are keen on recruiting young dynamic candidates to the PhD programme immediately. Those who hold a valid CSIR-JRF/ UGC-JRF/ ICMR category A/ DBT-JRF category A/ INSPIRE or equivalent fellowship should contact Dr. Mahalakshmi (maha[at]iiserb.ac.in).

    GRADUATE STUDENTS


    • Deepti Chaturvedi : OmpX-based methodology development for membrane protein studies; in vitro barrel engineering.

      Bharat Ramasubramanian Iyer : Biophysics and biochemistry of Salmonella OMPs.

      Muralikrishna Lella : Peptide chemistry, Mycobacteriophage peptide biophysics.

      Ankit Gupta : Yersinia and Mycobacterial membrane protein biophysics.

      Shubhangi Pandey : Human VDAC-2 structure-function studies.

      Shashank Ranjan Srivastava : Human VDAC-2 biophysics and barrel regulation.

      Achala Apte : Human VDAC-2 biophysics.

    BS-MS FINAL YEAR STUDENTS


    • Karuna Surendran: Membrane protein folding.

      Taniya Mary Binny: Membrane protein folding.

      Udit Aswal: Membrane protein folding.

    PROJECT RESEARCH FELLOWS


    • Aditya Narvekar: Ail biophysical studies.

      One position is open

    New Entrants


    • Nov 2016: We are keen on recruiting young dynamic candidates to the PhD program immediately. Those who hold a valid CSIR/UGC/ICMR-category A/INSPIRE or equivalent fellowship should contact Dr. Mahalakshmi (maha[at]iiserb.ac.in).

    OPENING FOR POSTDOCTORAL FELLOWS


    • May 2016: Applications are invited for the post of Postdoctoral Fellow in the following two research areas:

      Main area: Membrane protein folding. Qualification: Ph.D. in Biology [preferably, areas of Biochemistry or Biophysics] with experience in protein folding studies.

      Main area: Membrane protein engineering. Qualification: Ph.D. in Peptide Chemistry or Chemical Biology with experience in peptide synthesis, native chemical ligation and spectroscopic characterization.

      Candidates can send their complete CV with photograph and details of past publications to : maha[at]iiserb.ac.in. The area being applied to must be mentioned in the cover letter.

    Publications from IISERB (2012 - Present)


    • [35] Maurya, SR and Mahalakshmi, R*. Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities. Biol. Rev. 2016, In press (DOI: awaited).

      [34] Maurya, SR and Mahalakshmi, R*. Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific. Biochim. Biophys. Acta (Biomembranes) 2016, 1858(12): 2993-3004 (DOI: 10.1016/j.bbamem.2016.09.011).

      [33] Iyer, BR and Mahalakshmi, R*. Distinct structural elements govern folding, stability and catalysis in the outer membrane enzyme PagP. Biochemistry 2016, 55(35): 4960-4970 (DOI: 10.1021/acs.biochem.6b00678).

      [32] Iyer, BR#, Gupta, A# and Mahalakshmi, R*. Approaches for preparation and biophysical characterization of transmembrane beta-barrels. In Membrane Proteins: Chemical and Synthetic Approaches, Ed: Shukla AK, Springer Protocols Handbooks, Humana Press; 2016, Just accepted (DOI: awaited).

      [31] Lella, M and Mahalakshmi, R*. Engineering a Transmembrane Nanopore Ion Channel from a Membrane Breaker Peptide. J. Phys. Chem. Lett. 2016, 7(13): 2298-2303 (DOI: 10.1021/acs.jpclett.6b00987).

      [30] Lella, M and Mahalakshmi, R*. Solvation Driven Conformational Transitions in the Second Transmembrane Domain of Mycobacteriophage Holin. Biopolymers 2016, In press (DOI: 10.1002/bip.22894).

      [29] Makwana, KM and Mahalakshmi, R*. Capping beta-Hairpin with N-terminal D-Amino Acid Stabilizes Peptide Scaffold. Biopolymers 2016, 106: 260-266 (DOI: 10.1002/bip.22837).

      [28] de Pinto, V, Reina, S, Gupta, A, Messina, AA, Mahalakshmi, R. Role of cysteines in mammalian VDAC isoforms' function. Biochim. Biophys. Acta (Bioenergetics) 2016, 1857: 1219-1227 (DOI: 10.1016/j.bbabio.2016.02.020).

      [27] Reina, S, Checchetto, V, Saletti, R, Gupta, A, Chaturvedi, D, Guardiani, C, Guarino, F, Scorciapino, MA, Magri, A, Foti, S, Ceccarelli, M, Messina, AA, Mahalakshmi, R, Szabo, I and de Pinto, V. Unexpected Modifications of Cysteines in VDAC3: Indication that VDAC3 may Signal the Mitochondrial Intermembrane Redox State. Biophys. J. 2016, 110(3, S1): 19a (DOI: 10.1016/j.bpj.2015.11.162).

      [26] Makwana, KM and Mahalakshmi, R*. Stereopositional Outcome in the Packing of Dissimilar Aromatics in Designed beta-Hairpins. Chem. Eur. J. 2016, 22:4147-4156 (DOI: 10.1002/chem.201504428).

      [25] Lella, M, Kamilla, S, Jain, V* and Mahalakshmi, R*. Molecular Mechanism of Holin Transmembrane Domain I in Pore Formation and Bacterial Cell Death. ACS Chem. Biol. 2016, 11: 910-920 (DOI: 10.1021/acschembio.5b00875).

      [24] Maurya, SR and Mahalakshmi, R*. VDAC-2: Mitochondrial outer membrane regulator masquerading as a channel? FEBS J. 2016, 283: 1831-1836 (DOI: 10.1111/febs.13637).

      [23] Reina, S@, Checchetto, V@, Saletti, R, Gupta, A#, Chaturvedi, D#, Guardiani, C, Guarino, F, Scorciapino, MA, Magri, A, Foti, S, Ceccarelli, M*, Messina, AA*, Mahalakshmi, R*, Szabo, I* and de Pinto, V*. VDAC3 as a sensor of oxidative state of the intermembrane space of mitochondria: the putative role of cysteine residue modifications. Oncotarget 2016, 7:2249-2268 (DOI: 10.18632/oncotarget.6850). @,#Equal contribution.

      [22] Maurya, SR and Mahalakshmi, R*. N-helix and cysteines inter-regulate human mitochondrial VDAC-2 function and biochemistry. J. Biol. Chem. 2015, 290: 30240-30252 (DOI: 10.1074/jbc.M115.693978).

      [21] Makwana, KM and Mahalakshmi, R*. Implications of Aromatic-Aromatic Interactions: From Protein Structures to Peptide Models. Protein Sci. 2015, 24:1920-1933 (DOI: 10.1002/pro.2814).

      [20] Iyer, BR and Mahalakshmi, R*. Residue-dependent thermodynamic cost and barrel plasticity balances activity in the PhoPQ-activated enzyme PagP of Salmonella typhimurium Biochemistry 2015, 54:5712-5722 (DOI: 10.1021/acs.biochem.5b00543).

      [19] Makwana, KM and Mahalakshmi, R*. Structure Stabilizing Role of Aromatic Interactions is Decided by Spatial Arrangement of Aromatic Pairs: A Case Study With Designed Peptide beta-Hairpins. Peptides 2015, Proceedings of the 24th American Peptide Symposium, Eds: Srivastava V, Yudin A, Lebl M. 2015, American Peptide Society, San Diego, CA, pp 220-222 (DOI: 10.17952/24APS.2015.220).

      [18] Makwana, KM and Mahalakshmi, R*. Trp-Trp Cross-Linking: A Structure-Reactivity Relationship in the Formation and Design of Hyperstable Peptide beta-Hairpin and alpha-Helix Scaffolds. Org. Lett. 2015, 17:2498-2501 (DOI: 10.1021/acs.orglett.5b01017).

      [17] Makwana, KM and Mahalakshmi, R*. NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp - Trp Interactions in Designed beta-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for beta-Hairpin Capping. J. Phys. Chem. B 2015, 119: 5376-5385 (DOI: 10.1021/acs.jpcb.5b00554).

      [16] Mahalakshmi, R*. Folding and stability of transmembrane beta-barrels of bacterial and human origin: Probing underlying similarities and principal differences using in vitro systems. Proc. Indian Natn. Sci. Acad. 2015, 81(2): 463-478 (DOI: 10.16943/ptinsa/2015/v81i2/48099). Invited review.

      [15] Makwana, KM and Mahalakshmi, R*. Nature of aryl-tyrosine interactions contribute to beta-hairpin scaffold stability: NMR evidence for alternate ring geometry. Phys. Chem. Chem. Phys. 2015, 17: 4220-4230 (DOI: 10.1039/C4CP04991H).

      [14] Gupta, A, Iyer, BR, Chaturvedi, D#, Maurya, SR# and Mahalakshmi, R*. Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: Case study from bacteria and humans. R. Soc. Chem. Adv. 2015, 5(2): 1227-1234 (DOI: 10.1039/C4RA11207E). #Equal contribution.

      [13] Chaturvedi, D and Mahalakshmi, R*. Juxtamembrane tryptophans possess distinct roles in defining the OmpX barrel-micelle boundary and packing-facilitated protein-micelle association. FEBS Lett. 2014, 588: 4464-4471(DOI: 10.1016/j.febslet.2014.10.017).

      [12] Makwana, KM and Mahalakshmi, R*. Asymmetric contribution of aromatic interactions stems from spatial positioning of the interacting aryl pairs in beta-hairpins. ChemBioChem 2014, 15: 2357-2360 (DOI: 10.1002/cbic.201402340).

      [11] Gupta, A#, Zadafiya, P# and Mahalakshmi, R*. Differential Contribution of Tryptophans to the Folding and Stability of the Attachment Invasion Locus Transmembrane beta-Barrel from Yersinia pestis. Sci. Rep. 2014, 4: 6508 (DOI: 10.1038/srep06508). #Equal contribution.

      [10] Ravikiran, B and Mahalakshmi, R*. Unusual post-translational protein modifications : The benefits of sophistication. R. Soc. Chem. Adv. 2014, 4(64): 33958-33974 (DOI: 10.1039/C4RA04694C).

      [9] Maurya, SR and Mahalakshmi, R*. Cysteine Residues Impact the Stability and Micelle Interaction Dynamics of the Human Mitochondrial beta-barrel Anion Channel hVDAC-2. PLoS One 2014, 9(3): e92183 (DOI: 10.1371/journal.pone.0092183).

      [8] Makwana, KM and Mahalakshmi, R*. Comparative analysis of cross strand aromatic-Phe interactions in designed peptide beta-hairpins. Org. Biomol. Chem. 2014, 12(13): 2053-2061 (DOI: 10.1039/C3OB42247J). Selected for front cover illustration of issue.

      [7] Maurya, SR and Mahalakshmi, R*. Influence of Protein - Micelle Ratios and Cysteine Residues on the Kinetic Stability and Unfolding Rates of Human Mitochondrial VDAC-2. PLoS One 2014, 9(1): e87701 (DOI: 10.1371/journal.pone.0087701).

      [6] Chaturvedi, D and Mahalakshmi, R*. Methionine Mutations of Outer Membrane Protein X Influence Structural Stability and beta-Barrel Unfolding. PLoS One 2013, 8(11): e79351 (DOI: 10.1371/journal.pone.0079351).

      [5] Lella, M and Mahalakshmi, R*. Pro-Gly mediated conformational switch of Mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven. Chem. Commun. 2013, 49(83):9594-9596.

      [4] Makwana, KM, Raghothama, SR* and Mahalakshmi, R*. Stabilizing effect of electrostatic vs aromatic interactions in diproline nucleated peptide beta-hairpins. Phys. Chem. Chem. Phys. 2013, 15(37): 15321-15324. Selected as Hot Article.

      [3] Maurya, SR and Mahalakshmi, R*. Modulation of human mitochondrial voltage-dependent anion channel 2 (hVDAC-2) structural stability by cysteine-assisted barrel-lipid interactions. J. Biol. Chem. 2013, 288(35): 25584-25592.

      [2] Maurya, SR#, Chaturvedi, D#, Mahalakshmi, R*. Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel. Sci. Rep. 2013, 3:1989 (DOI: 10.1038/srep01989). #Equal contribution.

      [1] Gupta, A, Chaturvedi, D, Mahalakshmi, R*. Modified CNBr cleavage protocol for efficient separation of Met-Ser containing OmpX-Om14 membrane protein fusion. Intl. Rev. Biophys. Chem. 2012, 3(5): 147-156.

    Selected Publications (2004 - 2011)


      1. Plesniak, LA, Mahalakshmi, R, Rypien, C, Yang, Y, Racic, J and Marassi, FM. Expression, refolding, and initial structural characterization of the Y. pestis Ail outer membrane protein in lipids. Biochim. Biophys. Acta (Biomembranes) 2011, 1808: 482-489.
      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, 21: E76-E85.
      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 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 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., Humana Press; 2006, 340: 71-94.
      8. 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.
      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.

    MOLECULAR BIOPHYSICS LABORATORY : TEAM MEMBERS


    • Deepti Chaturvedi: OmpX-based methodology development for membrane protein studies and barrel engineering; hVDAC-2 engineering.

      Bharat Ramasubramanian Iyer: Biophysics and biochemistry of Salmonella OMPs; structure-function-stability studies.

      Muralikrishna Lella: Peptide chemistry, Mycobacteriophage peptide biophysics.

      Ankit Gupta: Yersinia and Mycobacterial membrane protein biophysics; hVDAC-3 biophysics.

      Shubhangi Pandey: Human VDAC-2 functional and regulational studies.

      Shashank Ranjan Srivastava: Human VDAC-2 biophysics and structural modulation under near-native conditions.

      Achala Apte: hVDAC-2 biophysical and functional studies.

      Aditya Narvekar: Ail biophysical studies.

    OPENING FOR POSTDOCTORAL FELLOWS


    • May 2016: Applications are invited for the post of Postdoctoral Fellow in the following two research areas:

      Main area: Membrane protein folding. Qualification: Ph.D. in Biology [preferably, areas of Biochemistry or Biophysics] with experience in protein folding studies.

      Main area: Membrane protein engineering. Qualification: Ph.D. in Peptide Chemistry or Chemical Biology with experience in peptide synthesis, native chemical ligation and spectroscopic characterization.

      Candidates can send their complete CV with photograph and details of past publications to : maha[at]iiserb.ac.in. The area being applied to must be mentioned in the cover letter.

    MOLECULAR BIOPHYSICS LABORATORY : PAST MEMBERS


    • [1] Dr. Kamlesh Madhusudan Makwana [currently postdoctoral fellow at Tufts University]

      [2] Dr. Svetlana Rajkumar Maurya