Professor Mehdi Mobli
Professor

Mehdi Mobli

Email: 
Phone: 
+61 7 334 60352

Background

Professor Mobli is a structural biologist and a group leader at the University of Queensland's Australian Institute for Bioengineering and Nanotechnology (AIBN). He is well known internationally for his contributions to the basic theory of multidimensional nuclear magnetic resonance and its applications to resolving the molecular structure of peptides and proteins, as well as studying their physiochemical properties and function. Mehdi's contributions to the field has been recognised by being appointed an Executive Editor of the AMPERE society's journal "Magnetic Resonance", and to the advisory board of the international Biological Magnetic Resonance Data Bank (BMRB) as well as serving on the board of directors of the Australia and New Zealand Society for Magnetic Resonance (ANZMAG). He is a former ARC Future Fellow and recipient of the ASBMB MERCK medal, the Australia Peptide Society's Tregear Award, the ANZMAG Sir Paul Callaghan medal and the Lorne Proteins Young Investigator Award (now Robin Anders Award).

Prof. Mobli's research group focuses on characterising the structure and function of receptors involved in neuronal signalling, with a particular focus on developing new approaches for the discovery and characterisation of modulators of these receptors through innovations in bioinformatics, biochemistry and and biophysics. This work has led to publication of more than 100 research articles attracting over 6,000 citations.

Availability

Professor Mehdi Mobli is:
Available for supervision
Media expert

Fields of research

Analytical biochemistry Analytical chemistry Bioinformatics and computational biology Biological Sciences Biomaterials Biomedical engineering Biomolecular modelling and design Characterisation of biological macromolecules Chemical Sciences Cheminformatics and quantitative structure-activity relationships Engineering Enzymes Information and Computing Sciences Macromolecular and materials chemistry Mathematical Sciences Medicinal and biomolecular chemistry Molecular medicine Numerical analysis Numerical and computational mathematics Optical properties of materials Organic chemistry Physical chemistry Physical organic chemistry Proteins and peptides Receptors and membrane biology Solution chemistry Structural biology (incl. macromolecular modelling) Theory of computation

Qualifications

  • Doctor of Philosophy, University of Liverpool

Research interests

  • Structure, function and dynamics of biomolecules studied in solution by NMR spectroscopy

    Nuclear magnetic resonance is one of the most powerful atomic resolution techniques for probing the physicochemical properties of molecules. In biophysics and particularly in protein research NMR can uniquely be used to determine both high-resolution structures and conformational dynamics of proteins in their natural solution state environment. NMR can further be used to provide functional data and is routinely used as a screening tool to provide input to structure based drug design studies. The properties that make NMR such a versatile technique also require technical expertise in data acquisition, analysis and interpretation. Dr Mobli's research is focused on the application of NMR spectroscopy in molecular biology, with the aim of increasing the utility of the technique itself through automation and also to expand its current applications. His group are working on diverse biological problems including understanding the structure of disulfide stabilised peptides, how voltage-gated ion channels are modulated by natural and synthetic ligands and the mechanism of bacterial transcription pausing. All of these projects are being pursued with the ultimate goal of developing novel drugs and diagnostic tools.

Research impacts

Bioactive peptides have long been recognised as important messengers in cellular communication and are integral to our understanding of basic physiological processes. Their potential as natural substrates for biological receptors has been leveraged successfully in some of the most important therapeutics of our time, such as insulin and oxytocin. In recent years, increased attention has been given to this molecular class due to the ease of generating large libraries of these peptides under selection pressure. This can yield potent drug leads through mRNA and phage display technologies. The potency and selectivity of these molecules come from their well-defined three-dimensional structures, which are often constrained by side-chain and/or backbone linkages that stabilise their 3D shape. Prof. Mobli's research group has contributed significantly to the understanding of the structure, dynamics, and function of constrained peptides. Our basic understanding of the physicochemical properties of bioactive peptides comes from studies of their structural and chemical properties. His group has directly contributed over 40 high-resolution structures of constrained peptides to the PDB, including arguably the highest resolution solution structure of a disulfide-constrained peptide to date (6URP). Detailed dynamic and functional studies have offered novel insights ranging from the basic chemistry of peptide side chains to the structural basis of peptide-receptor interactions and the evolution of neofunctionalisation of stable structural scaffolds.

Search Professor Mehdi Mobli’s works on UQ eSpace

146 works between 2003 and 2024
All (146) Journal Article (123) Book Chapter (11) Conference Publication (8) Book (3) Other Outputs (1)

121 - 140 of 146 works

2010

Journal Article

A non-uniformly sampled 4D HCC(CO)NH-TOCSY experiment processed using maximum entropy for rapid protein sidechain assignment

Mobli, Mehdi, Stern, Alan S., Bermel, Wolfgang, King, Glenn F. and Hoch, Jeffrey C. (2010). A non-uniformly sampled 4D HCC(CO)NH-TOCSY experiment processed using maximum entropy for rapid protein sidechain assignment. Journal of Magnetic Resonance, 204 (1), 160-164. doi: 10.1016/j.jmr.2010.02.012

A non-uniformly sampled 4D HCC(CO)NH-TOCSY experiment processed using maximum entropy for rapid protein sidechain assignment

2010

Conference Publication

Understanding the role of the unusual constrained eight-membered disulfide ring of spider toxins

Dantas de Araujo, A. D., Herzig, V., Mobli, M., Windley, M. J., Nicholson, G. M., Alewood, P. F. and King, G. F. (2010). Understanding the role of the unusual constrained eight-membered disulfide ring of spider toxins. 31st European Peptide Symposium, Copenhagen, Denmark, 5-9 September 2010. West Sussex, United Kingdom: John Wiley & Sons. doi: 10.1002/psc.1303

Understanding the role of the unusual constrained eight-membered disulfide ring of spider toxins

2010

Book Chapter

Determination of peptide and protein structures using NMR Spectroscopy

King, Glenn F and Mehdi Mobli (2010). Determination of peptide and protein structures using NMR Spectroscopy. Comprehensive natural products II: Chemistry and biology. (pp. 280-325) edited by Lewis Mander and Hung-Wen Liu. Oxford, England: Elsevier Science & Technology Books. doi: 10.1016/B978-008045382-8.00653-5

Determination of peptide and protein structures using NMR Spectroscopy

2010

Journal Article

Derivation of Peptide and Protein Structure using NMR Spectroscopy

King, Glenn F. and Mobli, Mehdi (2010). Derivation of Peptide and Protein Structure using NMR Spectroscopy. Comprehensive Natural Products Ii: Chemistry and Biology, Vol 9: Modern Methods in Natural Products Chemistry, 9, 279-325.

Derivation of Peptide and Protein Structure using NMR Spectroscopy

2009

Journal Article

Direct Visualization of Disulfide Bonds through Diselenide Proxies Using Se-77 NMR Spectroscopy

Mobli, M., Dantas de Araujo, A., Lambert, L. K., Pierens, G. K., Windley, M. J., Nicholson, G. M., Alewood, P. F. and King, G. E. (2009). Direct Visualization of Disulfide Bonds through Diselenide Proxies Using Se-77 NMR Spectroscopy. Angewandte Chemie International Edition, 48 (49), 9312-9314. doi: 10.1002/anie.200905206

Direct Visualization of Disulfide Bonds through Diselenide Proxies Using Se-77 NMR Spectroscopy

2009

Journal Article

Effective Protocol for Database Similarity Searching of Heteronuclear Single Quantum Coherence Spectra

Pierens, G. K., Mobli, M. and Vegh, V. (2009). Effective Protocol for Database Similarity Searching of Heteronuclear Single Quantum Coherence Spectra. Analytical Chemistry, 81 (22), 9329-9335. doi: 10.1021/ac901616t

Effective Protocol for Database Similarity Searching of Heteronuclear Single Quantum Coherence Spectra

2009

Journal Article

A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import

Kurabi, A, Brener, S, Mobli, M, Kwan, J. J. and Donaldson, L. W. (2009). A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import. Journal of Molecular Biology, 392 (5), 1168-1177. doi: 10.1016/j.jmb.2009.08.004

A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import

2009

Journal Article

Nonuniform sampling and spectral aliasing

Maciejewski, Mark W., Qui, Harry Z., Rujan, Iulian, Mobli, Mehdi and Hoch, Jeffrey C. (2009). Nonuniform sampling and spectral aliasing. Journal of Magnetic Resonance, 199 (1), 88-93. doi: 10.1016/j.jmr.2009.04.006

Nonuniform sampling and spectral aliasing

2009

Book Chapter

Maximum Entropy: Multidimensional Methods

Hoch, Jeffrey C. and Mobli, Mehdi (2009). Maximum Entropy: Multidimensional Methods. EMagRes. (pp. 1-8) United Kingdom: John Wiley & Sons. doi: 10.1002/9780470034590.emrstm1158

Maximum Entropy: Multidimensional Methods

2008

Journal Article

Maximum entropy spectral reconstruction of nonuniformly sampled data

Mobli, Mehdi and Hoch, Jeffrey C. (2008). Maximum entropy spectral reconstruction of nonuniformly sampled data. Concepts in Magnetic Resonance Part A, 32A (6), 436-448. doi: 10.1002/cmr.a.20126

Maximum entropy spectral reconstruction of nonuniformly sampled data

2008

Book

Modelling H NMR Spectra of Organic Compounds: Theory, Applications and NMR Prediction Software

Abraham, Raymond J. and Mobli, Mehdi (2008). Modelling H NMR Spectra of Organic Compounds: Theory, Applications and NMR Prediction Software. Chichester, UK: John Wiley and Sons. doi: 10.1002/9780470721803

Modelling H NMR Spectra of Organic Compounds: Theory, Applications and NMR Prediction Software

2008

Journal Article

The structural plasticity of heparan sulfate NA-domains and hence their role in mediating multivalent interactions is confirmed by high-accuracy 15N-NMR relaxation studies

Mobli, Mehdi, Nilsson, Mathias and Almond, Andrew (2008). The structural plasticity of heparan sulfate NA-domains and hence their role in mediating multivalent interactions is confirmed by high-accuracy 15N-NMR relaxation studies. Glycoconjugate Journal, 25 (5), 401-414. doi: 10.1007/s10719-007-9081-9

The structural plasticity of heparan sulfate NA-domains and hence their role in mediating multivalent interactions is confirmed by high-accuracy 15N-NMR relaxation studies

2008

Conference Publication

Unequivocal direct determination of the disulfide bond connectivities in proteins using 77Se NMR

Mobli, M., Lambert, L. K., Pierens, G. K., Dantas de Araujo, A., Alewood, P. F. and King, G. F. (2008). Unequivocal direct determination of the disulfide bond connectivities in proteins using 77Se NMR. 7th Biennial Conference of the Australian and New Zealand Society for Magnetic Resonance (ANZMAG 2008), Couran Cove, Australia, 7-11 December 2008.

Unequivocal direct determination of the disulfide bond connectivities in proteins using 77Se NMR

2008

Book

Modelling 1H NMR spectra of organic compounds: Theory, applications and NMR prediction software

Abraham, Raymond and Mobli, Mehdi (2008). Modelling 1H NMR spectra of organic compounds: Theory, applications and NMR prediction software. Chichester: Wiley.

Modelling 1H NMR spectra of organic compounds: Theory, applications and NMR prediction software

2007

Journal Article

An NMR, IR and theoretical investigation of 1H Chemical Shifts and hydrogen bonding in phenols

Abraham, Raymond J. and Mobli, Mehdi (2007). An NMR, IR and theoretical investigation of 1H Chemical Shifts and hydrogen bonding in phenols. Magnetic resonance in chemistry, 45 (10), 865-877. doi: 10.1002/mrc.2060

An NMR, IR and theoretical investigation of 1H Chemical Shifts and hydrogen bonding in phenols

2007

Journal Article

Automatic maximum entropy spectral reconstruction in NMR

Mobli, Mehdi, Maciejewski, Mark W., Gryk, Michael R. and Hoch, Jeffrey C. (2007). Automatic maximum entropy spectral reconstruction in NMR. Journal of Biomolecular NMR, 39 (2), 133-139. doi: 10.1007/s10858-007-9180-8

Automatic maximum entropy spectral reconstruction in NMR

2007

Journal Article

An automated tool for maximum entropy reconstruction of biomolecular NMR spectra

Mobli, Mehdi, Maciejewski, Mark W., Gryk, Michael R. and Hoch, Jeffrey C. (2007). An automated tool for maximum entropy reconstruction of biomolecular NMR spectra. Nature Methods, 4 (6), 467-468. doi: 10.1038/nmeth0607-467

An automated tool for maximum entropy reconstruction of biomolecular NMR spectra

2007

Journal Article

N-Acetylated amino sugars: the dependence of NMR 3J(HNH2)-couplings on conformation, dynamics and solvent

Mobli, Mehdi and Almond, Andrew (2007). N-Acetylated amino sugars: the dependence of NMR 3J(HNH2)-couplings on conformation, dynamics and solvent. Organic and biomolecular chemistry, 5 (14), 2243-2251. doi: 10.1039/b705761j

N-Acetylated amino sugars: the dependence of NMR 3J(HNH2)-couplings on conformation, dynamics and solvent

2006

Journal Article

Spectral reconstruction methods in fast NMR: Reduced dimensionality, random sampling and maximum entropy

Mobli, Mehdi, Stern, Alan S. and Hoch, Jeffrey C. (2006). Spectral reconstruction methods in fast NMR: Reduced dimensionality, random sampling and maximum entropy. Journal of magnetic resonance, 182 (1), 96-105. doi: 10.1016/j.jmr.2006.06.007

Spectral reconstruction methods in fast NMR: Reduced dimensionality, random sampling and maximum entropy

2006

Journal Article

Three-Dimensional 13C-Detected CH3-TOCSY Using Selectively Protonated Proteins: Facile Methyl Resonance Assignment and Protein Structure Determination

Jordan, John B., Kovacs, Helena, Wang, Yuefeng, Mobli, Mehdi, Luo, Rensheng, Anklin, Clemens, Hoch, Jeffrey C. and Kriwacki, Richard W. (2006). Three-Dimensional 13C-Detected CH3-TOCSY Using Selectively Protonated Proteins: Facile Methyl Resonance Assignment and Protein Structure Determination. Journal of the American Chemical Society, 128 (28), 9119-9128. doi: 10.1021/ja058587a

Three-Dimensional 13C-Detected CH3-TOCSY Using Selectively Protonated Proteins: Facile Methyl Resonance Assignment and Protein Structure Determination

Current funding

  • 2024 - 2025
    A national network for magnetic resonance spectroscopy
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2024 - 2027
    Defining a new family of sodium channel accessory proteins
    ARC Discovery Projects
    Open grant

Past funding

  • 2023 - 2024
    High-Resolution Electron Paramagnetic Resonance Imaging and Spectroscopy
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2022 - 2025
    Autocyclases: A new class of self-cyclising proteins
    ARC Discovery Projects
    Open grant
  • 2021 - 2023
    Bivalent analgesics: rational design of selective ion channel inhibitors with optimised mechanism of action
    NHMRC IDEAS Grants
    Open grant
  • 2019 - 2022
    A new source of bivalent molecules from nature
    ARC Discovery Projects
    Open grant
  • 2019 - 2022
    Accessing structurally elusive states of sodium channels as novel analgesic targets
    NHMRC Project Grant
    Open grant
  • 2019
    Chemical Purification Network
    UQ Major Equipment and Infrastructure
    Open grant
  • 2019
    Imaging Mass Spectrometry at Higher Mass Resolution
    UQ Research Facilities Infrastructure Grants
    Open grant
  • 2019 - 2021
    Molecular basis and inhibition of TIR-domain function in Toll-like receptor and neuronal cell-death pathways
    NHMRC Project Grant
    Open grant
  • 2018
    High-throughput ion channel pharmacology
    UQ Major Equipment and Infrastructure
    Open grant
  • 2018
    In vivo optical imaging into the next generation
    UQ Research Facilities Infrastructure Grants
    Open grant
  • 2018
    Multichannel peptide synthesiser to accelerate UQ's biodiscovery pipeline and peptide drug development programs
    UQ Major Equipment and Infrastructure
    Open grant
  • 2017 - 2019
    Targeting voltage sensing for drug development
    UQ Development Fellowships
    Open grant
  • 2016 - 2017
    A nuclear magnetic resonance facility for modern molecular analysis
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2016 - 2018
    A pharmacological approach to define the contribution of Nav1.7 to pain pathways
    NHMRC Project Grant
    Open grant
  • 2016 - 2018
    Characterization and inhibition of higher-order assembly signalling in Toll-like receptor pathways
    NHMRC Project Grant
    Open grant
  • 2016
    Patch-clamp electrophysiology platform for drug and insecticide discovery
    UQ Major Equipment and Infrastructure
    Open grant
  • 2015
    Protein Analysis Facility
    UQ Major Equipment and Infrastructure
    Open grant
  • 2015 - 2018
    Understanding how toxins interact with lipid membranes and ion channels
    NHMRC Project Grant
    Open grant
  • 2014 - 2017
    Unravelling the structural complexity of ancient Australian arthropod venoms
    ARC Discovery Projects
    Open grant
  • 2012 - 2016
    ASAP-NMR: A leap forward in structural studies of proteins using NMR spectroscopy
    ARC Future Fellowships
    Open grant
  • 2012 - 2014
    Rational development of novel analgesics for the treatment of chronic pain
    NHMRC Project Grant
    Open grant
  • 2010
    High-throughput identification and structural characterization of selective Nav1.7 channel ligands; a prime target in the treatment of pain
    UQ Early Career Researcher
    Open grant

Availability

Professor Mehdi Mobli is:
Available for supervision

Before you email them, read our advice on how to contact a supervisor.

Supervision history

Current supervision

  • Doctor Philosophy

    Studies of complex biomolecular systems using advanced biochemical and biophysical techniques

    Principal Advisor

    Other advisors: Associate Professor Jeffrey Harmer

  • Doctor Philosophy

    Structural and functional characterisation of an orphan family of opioid peptides

    Principal Advisor

    Other advisors: Associate Professor Jody Peters

  • Doctor Philosophy

    The ASIC thumb domain as a channel proxy for identification of drug leads for the treatment of ischemic conditions

    Principal Advisor

    Other advisors: Dr Lachlan Rash

  • Doctor Philosophy

    Fast Acquisition Methods in Multidimensional NMR

    Principal Advisor

  • Doctor Philosophy

    Characterisation of the lipid dependent gating of voltage gated ion channels

    Principal Advisor

  • Doctor Philosophy

    Accessing structurally elusive states of sodium channels as novel analgesic targets

    Principal Advisor

    Other advisors: Professor Irina Vetter, Dr Thomas Durek

  • Doctor Philosophy

    Fast Acquisition Methods in Multidimensional NMR

    Principal Advisor

  • Doctor Philosophy

    Modulation of opioid catabolism by endogenous neuropeptides

    Principal Advisor

  • Doctor Philosophy

    Analysis of Complex Metabolomic Data

    Associate Advisor

  • Doctor Philosophy

    Understanding the function of sodium channel accessory proteins to develop new treatments for chronic pain

    Associate Advisor

    Other advisors: Dr Jennifer Deuis, Professor Irina Vetter

  • Doctor Philosophy

    Complex Data Analysis Problems in NMR-based Metabolomics

    Associate Advisor

  • Doctor Philosophy

    Structural and biochemical characterization of dual enzymatic activity of TIR domains from plant innate immune receptors

    Associate Advisor

    Other advisors: Dr Natsumi Maruta, Professor Bostjan Kobe

  • Doctor Philosophy

    Characterization of bivalency in disulfide-rich peptides

    Associate Advisor

    Other advisors: Professor Irina Vetter

  • Doctor Philosophy

    Discovery and characterisation of multi-valent peptides

    Associate Advisor

    Other advisors: Professor Irina Vetter

Completed supervision

Enquiries

Contact Professor Mehdi Mobli directly for media enquiries about:

  • Mechanism of voltage gating by voltage-gated ion channels
  • Structure guided drug design
  • Structure guided evolution of venom peptides

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