Department of Biological Sciences
Indian Institute of Science Education and Research Bhopal


Personal Details


  • Name: Dr. R. Mahalakshmi
  • Designation: Associate Professor
  • Department: Biological Sciences
  • E-Mail: maha[AT]iiserb.ac.in
  • Phone: +91 755 269 1423, 669 1423


Awards and Fellowships


  • 2017 : SERB Women Excellence Award
  • 2015 - Present: Wellcome Trust/ DBT India Alliance Intermediate Fellow
  • 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 Fellowship.

Academic Details


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


  • APRIL 2017: We are keen on selecting candidates who are highly motivated and committed to research. Those who hold a valid CSIR-JRF/ UGC-JRF/ ICMR- category A/ DBT-JRF/ DST-INSPIRE or equivalent fellowship should contact Dr. Mahalakshmi (maha[at]iiserb.ac.in).

Cellular life requires chiral biomacromolecules such as proteins to be retained in their native folded state. While evolution has coded specific folding pathways in the protein primary sequence and provided molecular foldases to assist protein folding, an energetically favourable consequence of protein misfolding is aggregation. Protein aggregation is the causative agent for several known neurodegenerative diseases. Membrane proteins are particularly enriched with hydrophobic residues that make them vulnerable to aggregation. Hence, membrane protein biogenesis is a considerably challenging process within the aqueous environment of the cell. Therefore, it is pertinent to deduce the structural, biochemical, and thermodynamic principles that decide the outcome of membrane protein folding versus aggregation, at the molecular level. Simply put, it is important to understand the fundamental mechanism of membrane protein biogenesis.





Membrane proteins constitute ~30% of the cell’s proteome and are involved in every cellular process. Transmembrane beta-barrels of the mitochondrial outer membrane are particularly important for metabolite transport, sequestering misfolded proteins and, in addition to maintaining cell homeostasis, are also implicated in ROS suppression, aging, cancer, and neurodegenerative diseases. I am interested in understanding the biogenesis of mitochondrial transmembrane beta-barrels at the molecular level. One of the biologically relevant proteins I study is the Voltage- Dependent Anion Channel (VDAC), found in the mitochondrial outer membrane. Other mitochondrial beta-barrels I plan to study include Sam50 (50kDa subunit of the Sorting and Assembly Machinery complex), and Tom40 (core protein of the Translocase of the Outer Mitochondrial membrane complex). Additionally, I also employ outer membrane proteins from pathogenic bacteria as model systems, including the Ail (Attachment invasion locus) protein from Yersinia pestis, PagP (PhoPQ-activated gene P) from Salmonella typhimurium, and BamA (main component of the beta-Barrel Assembly Machinery). Using biophysical and spectroscopic tools, I am working towards the identification of key residues that stabilize transmembrane beta-barrels and are important for their unique functions within the cell.


The goal of research in my laboratory is to identify a functional link between proteostasis, membrane protein remodelling and quality control, and occurrence of disease states.


Authors Title of Article Journal Year
Deepti Chaturvedi
Radhakrishnan Mahalakshmi
Position–specific contribution of interface tryptophans on membrane protein energetics Biochim. Biophys. Acta (Biomembranes) 2018
Muralikrishna Lella
Radhakrishnan Mahalakshmi
Solvation Driven Conformational Transitions in the Second Transmembrane Domain of Mycobacteriophage Holin. Biopolymers 2017
Bharat Ramasubramanian Iyer
Ankit Gupta
Radhakrishnan Mahalakshmi
Approaches for preparation and biophysical characterization of transmembrane β-barrels Springer Protocols Handbooks 2017
Muralikrishna Lella
Radhakrishnan Mahalakshmi
Metamorphic Proteins: Emergence of dual protein folds from one primary sequence. Biochemistry 2017
Bharat Iyer
Punit Zadafiya
Pallavi Vetal
Radhakrishnan Mahalakshmi
Energetics of side chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein. Journal of Biological Chemistry 2017
Svetlana Maurya
Radhakrishnan Mahalakshmi
Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities. Biological Reviews 2017
Radhakrishnan Mahalakshmi
Svetlana Maurya
Bhavna Burdak
Parini Surti
Manoj Patel
Vikas Jain
Structural plasticity of T4 transcription co-activator gp33 revealed by a protease-resistant unfolded state Biophysical and Biochemical Research Communication 2017
Deepti Chaturvedi
Radhakrishnan Mahalakshmi
Transmembrane β-barrels: Evolution, folding and energetics. Biochim. Biophys. Acta (Biomembranes) 2017
Muralikrishna Lella
Radhakrishnan Mahalakshmi
Engineering a Transmembrane Nanopore Ion Channel from a Membrane Breaker Peptide. The Journal of Physical Chemistry Letters 2016
Svetlana Maurya
Radhakrishnan Mahalakshmi
Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific. Biochim. Biophys. Acta (Biomembranes) 2016
Simona Reina
Vanessa Checchetto
Rosaria Saletti
Ankit Gupta
Deepti Chaturvedi
Carlo Guardiani
Francesca Guarino
Mariano Andrea Scorciapino
Andrea Magrì
Salvatore Foti
Matteo Ceccarelli
Angela Anna Messina
Radhakrishnan Mahalakshmi
Ildiko Szabo
Vito De Pinto
VDAC3 as a sensor of oxidative state of the intermembrane space of mitochondria: the putative role of cysteine residue modifications. Oncotarget 2016
Svetlana Rajkumar Maurya
Radhakrishnan Mahalakshmi
VDAC-2: Mitochondrial outer membrane regulator masquerading as a channel? FEBS Journal 2016
Muralikrishna Lella
Soumya Kamilla
Vikas Jain
Radhakrishnan Mahalakshmi
Molecular Mechanism of Holin Transmembrane Domain I in Pore Formation and Bacterial Cell Death. ACS Chemical Biology 2016
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
Stereopositional Outcome in the Packing of Dissimilar Aromatics in Designed beta-Hairpins Chemistry - A European Journal 2016
Simona Reina
Vanessa Checchetto
Rosaria Saletti
Ankit Gupta
Deepti Chaturvedi
Carlo Guardiani
Francesca Guarino
Mariano Andrea Scorciapino
Andrea Magrì
Salvatore Foti
Matteo Ceccarelli
Angela A. Messina
Radhakrishnan Mahalakshmi
Ildiko Szabo
Vito De Pinto
Unexpected Modifications of Cysteines in VDAC3: Indication that VDAC3 may Signal the Mitochondrial Intermembrane Redox State Biophysical Journal 2016
Vito De Pinto
Simona Reina
Ankit Gupta
Angela Messina
Radhakrishnan Mahalakshmi
Role of cysteines in mammalian VDAC isoforms' function. Biochim. Biophys. Acta (Bioenergetics) 2016
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
Capping beta-Hairpin with N-terminal D-Amino Acid Stabilizes Peptide Scaffold. Biopolymers 2016
Ankit Gupta
Bharat Ramasubramanian Iyer
Deepti Chaturvedi
Svetlana Rajkumar Maurya
Radhakrishnan Mahalakshmi
Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: Case study from bacteria and humans. RSC Advances 2015
Kamlesh Makwana
Radhakrishnan Mahalakshmi
Nature of aryl-tyrosine interactions contribute to beta-hairpin scaffold stability: NMR evidence for alternate ring geometry. Phys. Chem. Chem. Phys. 2015
Radhakrishnan Mahalakshmi
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
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
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
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
Trp-Trp Cross-Linking: A Structure-Reactivity Relationship in the Formation and Design of Hyperstable Peptide beta-Hairpin and alpha-Helix Scaffolds. Organic Letters 2015
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
Structure Stabilizing Role of Aromatic Interactions is Decided by Spatial Arrangement of Aromatic Pairs: A Case Study With Designed Peptide beta-Hairpins. Peptides 2015
Bharat Ramasubramanian Iyer
Radhakrishnan Mahalakshmi
Residue-dependent thermodynamic cost and barrel plasticity balances activity in the PhoPQ-activated enzyme PagP of Salmonella typhimurium Biochemistry 2015
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
Implications of Aromatic-Aromatic Interactions: From Protein Structures to Peptide Models. Protein Science 2015
Svetlana Rajkumar Maurya
Radhakrishnan Mahalakshmi
N-helix and cysteines inter-regulate human mitochondrial VDAC-2 function and biochemistry. Journal of Biological Chemistry 2015
Svetlana Rajkumar Maurya
Radhakrishnan Mahalakshmi
Influence of Protein - Micelle Ratios and Cysteine Residues on the Kinetic Stability and Unfolding Rates of Human Mitochondrial VDAC-2 PLoS One 2014
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
Comparative analysis of cross strand aromatic-Phe interactions in designed peptide beta-hairpins. Organic & Biomolecular Chemistry 2014
Svetlana Rajkumar Maurya
Radhakrishnan Mahalakshmi
Cysteine Residues Impact the Stability and Micelle Interaction Dynamics of the Human Mitochondrial beta-barrel Anion Channel hVDAC-2. PLoS One 2014
Ravikiran Boddepalli
Radhakrishnan Mahalakshmi
Unusual post-translational protein modifications : The benefits of sophistication. RSC Advances 2014
Ankit Gupta
Punit Zadafiya
Radhakrishnan Mahalakshmi
Differential Contribution of Tryptophans to the Folding and Stability of the Attachment Invasion Locus Transmembrane beta-Barrel from Yersinia pestis. Scientific Reports 2014
Kamlesh Madhusudan Makwana
Radhakrishnan Mahalakshmi
Asymmetric contribution of aromatic interactions stems from spatial positioning of the interacting aryl pairs in beta-hairpins ChemBioChem 2014
Deepti Chaturvedi
Radhakrishnan Mahalakshmi
Juxtamembrane tryptophans possess distinct roles in defining the OmpX barrel-micelle boundary and packing-facilitated protein-micelle association FEBS Lett. 2014
Svetlana Rajkumar Maurya
Deepti Chaturvedi
Radhakrishnan Mahalakshmi
Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel Scientific Reports 2013
Svetlana Rajkumar Maurya
Radhakrishnan Mahalakshmi
Modulation of human mitochondrial voltage-dependent anion channel 2 (hVDAC-2) structural stability by cysteine-assisted barrel-lipid interactions. Journal of Biological Chemistry 2013
Kamlesh Madhusudan Makwana
SR Raghothama
Radhakrishnan Mahalakshmi
Stabilizing effect of electrostatic vs aromatic interactions in diproline nucleated peptide beta-hairpins. Phys. Chem. Chem. Phys. 2013
Muralikrishna Lella
Radhakrishnan Mahalakshmi
Pro-Gly mediated conformational switch of Mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven. Chemical Communications 2013
Deepti Chaturvedi
Radhakrishnan Mahalakshmi
Methionine Mutations of Outer Membrane Protein X Influence Structural Stability and beta-Barrel Unfolding. PLoS One 2013
Ankit Gupta
Deepti Chaturvedi
Radhakrishnan Mahalakshmi
Modified CNBr cleavage protocol for efficient separation of Met-Ser containing OmpX-Om14 membrane protein fusion Intl. Rev. Biophys. Chem. 2012

Molecular Biophysics Laboratory Members


GROUP LEADER: Dr. Radhakrishnan Mahalakshmi, PhD
(Associate Professor and Wellcome Trust/ DBT India Alliance Intermediate Fellow)
  • Deepti Chaturvedi (PhD student)
  • Bharat Ramasubramanian Iyer (PhD student)
  • Muralikrishna Lella (PhD student)
  • Ankit Gupta (PhD student)
  • Shubhangi Pandey (PhD student)
  • Shashank Ranjan Srivastava (PhD student)
  • Dr. Muniyappa Krishnamurthy (Postdoctoral fellow)
  • Udit Aswal (BSMS student)
  • Taniya Mary Binny (BSMS student)
  • Karuna Surendran (BSMS student)

Opening for PhD students


  • APRIL 2017: We are keen on selecting candidates who are highly motivated and committed to research. Those who hold a valid CSIR-JRF/ UGC-JRF/ ICMR- category A/ DBT-JRF/ DST-INSPIRE or equivalent fellowship should contact Dr. Mahalakshmi (maha[at]iiserb.ac.in).

Opening for Postdoctoral Fellows


APRIL 2017: Applications are invited for the post of Postdoctoral Fellow in the following two research areas:
  • Main area: Deducing the assisted and unassisted assembly mechanism of transmembrane beta-barrels from human mitochondria.
    Qualification: Ph.D. in Biology [preferably, areas of Biochemistry or Biophysics] with experience in protein folding studies.
  • Main area: Design and engineering of membrane proteins for application in nanotechnology.
    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.

Opening for Project Research Fellows


  • Upto two positions are available. Only enthusiastic and committed students need apply.