A combination of physical and chemical processes works to maintain life.Biochemistry deals with these complex processes. In order to have a better understanding of the logic of life one needs to know about the structure of biomolecules and the way they interact with each other.

Physical biochemistry uses a variety of physical techniques to study the structure of biological function of the molecules in living organisms. There are methods to determine the structure of biomolecules. Other methods are used to study the interaction of biomolecules with each other and their enviornment. Instruments in a physical biochemistry laboratory can include NMR, IR, CD and fluorescence spectrometers, calorimeters and molecular modelling workstations.

My research interests are in the chemical synthesis and de novo design of peptides and proteins, solution and membrane structures of peptide and protein pore-formers, energetics and mechanism of interaction of peptides and proteins with biological membranes and the implied role of biomembrane architecture, functional aspects and dynamism of peptide and protein ion channels and carriers (including the mechanisms of ion transfer through membranes), protein folding mechanisms in solution and membrane milieus, molecular modelling of biomolecules, and peptide antibiotics.

Selected Recent Publications:

1) ‘Trans-bilayer ion conduction by proline containing cyclic hexapeptides and effects of amino acid substitutions on ion conducting properties’,  J. Taira, S. Osada, R. Hayashi, T. Ueda, M. Jelokhani-Niaraki, H. Aoyagi and H Kodama, Bull. Chem. Soc. Japan 83: 683-688 (2010)

2) ‘Ion channel activity of transmembrane segment 6 of Escherichia coli proton-dependent manganese transporter’, V. Ňuňuková, E. Urbánková, M. Jelokhani-Niaraki and R. Chaloupka, Biopolymers 93: 718-726 (2010)

3) ‘A comparative study on conformation and ligand binding of the neuronal uncoupling  proteins', M.V. Ivanova, T. Hoang, F.R. McSorley, G. Krnac, M.D. Smith and M. Jelokhani-Niaraki, Biochemistry 49: 512-521 (2010)

4) ‘The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains’, L.G.-L. Richardson, M. Jelokhani-Niaraki and M.D. Smith, BMC Biochemistry 10: 35 (1-8) (2009)

5) ‘Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides’, M. Jelokhani-Niaraki, L.H. Kondejewski, L.C. Wheaton and R.S. Hodges, J. Med. Chem. 52: 2090-2097 (2009)

6) ‘Chiral thiol-stabilized silver nanoclusters with well-resolved optical transitions synthesized by a facile etching procedure in aqueous solutions’, N. Cathcart, P. Mistry, C. Makra, B. Pietrobon, N. Coombs, M. Jelokhani-Niaraki, and V. Kitaev, Langmuir 25: 5840-5846 (2009)

7) ‘Interaction of gramicidin S and its aromatic amino acid analogs with phospholipid membranes’, M. Jelokhani-Niaraki, R.S. Hodges, J.E. Meissner, U.E. Hassenstein and L. Wheaton, Biophys. J. 95: 3306-3321 (2008)

8) ‘A CD study of uncoupling protein-1 and its transmembrane and matrix-loop domains’, M. Jelokhani-Niaraki, M.V. Ivanova, B.L. McIntyre, C.L. Newman, F.R. McSorley, E.K. Young and M.D. Smith, Biochem. J. 411: 593-603 (2008)

9) ‘Ion-Channel formation assisted by electrostatic interhelical interactions in covalently dimerized amphiphilic helical peptides’, J. Taira, M. Jelokhani-Niaraki, S. Osada, F. Kato and H. Kodama, Biochemistry 47: 3705-3714 (2008)

10) ‘Structure-activity relationships of diastereomeric lysine ring size analogs of the antimicrobial peptide gramicidin S’, E. J. Prenner, M. Kiricsi, , M. Jelokhani-Niaraki, R. N. A. H. Lewis, R. S. Hodges and R. N. McElhaney, J. Biol. Chem. 280: 2002-2011 (2005)

11) ‘Second transmembrane domain of human uncoupling protein 2 is essential for its ion channel formation’, H.Yamaguchi, M. Jelokhani-Niaraki and H. Kodama, FEBS Letts. 577: 299-304 (2004)