Staff Profile


Dr Marieke Bloemink

Senior Lecturer

School: School of Human and Life Sciences

Campus: Canterbury

Tel: 01227 922431

Profile summary

Dr Marieke Bloemink joined CCCU in October 2013 as a senior lecturer in Chemistry and Biology. She obtained her PhD in Bio-inorganic Chemistry at Leiden University, The Netherlands where she studied the interactions between anticancer platinum drugs and DNA. After her PhD she moved to the United States where she worked on zinc finger proteins, implicated in HIV, at Virginia Commonwealth University (Richmond, VA) and on the phosphorylation of ribosomal protein L18 at Yale University (New Haven, CT). She subsequently moved to Kent University (Canterbury, UK) and solved the NMR structure of MBP70, a key protein implicated in tuberculosis, after which she started to work on the kinetics and structure of myosin and other molecular motors.

Current research interests involve the biochemistry of muscle contraction, cardiac disease and muscle ageing.

Research and knowledge exchange

Myosin light chains.

Force development during contraction of the heart is crucial for optimal cardiac function. Myosin light chain proteins are involved in this process but their exact role is not clear. In healthy hearts different types of myosin light chains work together to optimise the force production, whereas in diseased hearts this process is disrupted. Patients with chronic heart failure show changes in concentrations of various light chains, and inherited changes (mutations) in cardiac light chains have been linked to hypertrophic cardiomyopathy, a serious heart condition that can result in sudden death. My research investigates the structure and function of different cardiac light chains using biochemical and biophysical techniques in order to understand how they work in healthy hearts and in diseased hearts.

Muscle ageing.

Recently, we have started to look at the molecular mechanisms involved in muscle ageing (sarcopenia), both at a molecular level but also at whole organism level (C. elegans) in collaboration with Dr Simon Harvey and Dr Jana Stastna. We use nematodes that express fluorescently labelled muscle proteins to investigate the muscle ageing process and factors that can affect this process.


Teaching and subject expertise

Teaching Responsibilities:

Modules which have a chemistry or biochemistry component, such as Foundation Chemistry, Core Science (level 4), Chemistry for the Life Sciences (level 5), Chemistry for the Environmental Sciences (level 5) and Applied Biological Chemistry (level 6).


Professional Memberships:

Fellow of the Higher Education Academy

Member of the Royal Society of Chemistry, the British Biochemical Society, the American Association for the Advancement of Science (AAAS) and the Biophysical Society.

External activities

Poster: "The ventricular cardiac myosin essential light chain (ELCv) recognizes the IQ1 binding site using a two-step mechanism". at the ‘Myosin, Muscle and many other motors’ Alpbach meeting 2016 in Austria.

Talk: “Of mice, muscle and men. Adaptation of myosin molecules for movement and force generation”. AMC conference 2015, Canterbury, UK

Poster: “Interaction between converter residue R759 and relay loop residue N509 in Drosophila muscle myosin is critical for optimal myosin function". Muscle and Molecular Motors Gordon Research Conference 2014, Vermont, USA.

Talk: “The hypertrophic cardiomyopathy mutation R453C alters the kinetic properties of human β-myosin”, at the ‘Myosin, Muscle and many other motors’ Alpbach meeting 2013 in Austria.

Talk: “Kinetic analysis of skeletal and cardiac human myosin isoforms”, at the ‘European Muscle Conference 2012 in Rhodes, Greece.

Poster (x2): 1. “Kinetic Characterization of Converter and Relay Loop Domain Interaction In Drosophila Myosin Sub-Fragment 1” and 2.”Fast Kinetic Analysis of Human Myosin Motors in Health and DiseaseBiophysical Society meeting 2012 in San Diego, USA.

Talk: “Kinetic analysis of human cardiac α- and β-myosin isoforms” at the 15th London Muscle Conference 2011, London, UK.

Publications and research outputs

  1. Bloemink, M.J., Melkani, G.C., Bernstein, S.I. Geeves, M.A. The Relay/Converter Interface Influences Hydrolysis of ATP by Skeletal Muscle Myosin II,” J. Biol. Chem. (2016), 291, 1763-1773.
  2. Walklate J, Vera, C, Bloemink MJ, Geeves MA, Leinwand LA (2016), ‘The Most Prevalent Freeman-Sheldon Syndrome Mutations in the Embryonic Myosin Motor Share Functional Defects’ Journal of Biological Chemistry 291, 10318-10331
  3. Bloemink, M.J., Deacon, JC, Langer, S., Vera, C, Combs, A., Leinwand, L.A., Geeves, M.A. The Hypertrophic Cardiomyopathy Myosin Mutation R453C Alters ATP Binding and Hydrolysis of Human Cardiac β-Myosin,” J. Biol. Chem. (2014), 289, 5158-5167.
  4. Bloemink, M.J., Deacon, JC, Resnicow, D.I., Leinwand, L.A., Geeves, M.A.The superfast extra-ocular myosin is kinetically distinct from the fast skeletal IIa, IIb and IId isoforms,” J. Biol. Chem. (2013), 288, 27469-27479.
  5. Deacon, J.C.,  Bloemink, M.J., Rezavandi, H, Leinwand, L.A., Geeves, M.A.Identification of functional differences between recombinant human α and β cardiac myosin motors,” Cell.Mol.Life Sci. (2012), 69, 2261-2277.
  6. Bloemink, M.J., Melkani, G.C., Dambacher, C.M., Bernstein, S.I. Geeves, M.A. Two Drosophila Myosin transducer mutants with distinct cardiomyopathies have divergent ADP and actin affinities,” J. Biol. Chem. (2011), 286, 28435-28443.
  7. Bloemink, M.J. and Geeves, M.A. “Shaking the myosin family tree: biochemical kinetics defines four types of myosin motor” , Semin. Cell Devel. Biol. (2011), 22, 961-967.
  8. Bloemink, M.J., Dambacher, C.M., Knowles, A.F., Melkani, G.C., Geeves, M.A. and Bernstein, S.I.Alternative Exon 9-Encoded Relay Domains Affect More than One Communication Pathway in the Drosophila Myosin HeadJ. Mol. Biol. (2009), 389, 707-721.
  9. Albet-Torres, N., Bloemink*, M.J., Barman, T., Candau, R., Frolander, K., Geeves, M.A., Golker, K., Herrmann, C., Lionne, C., Piperio, C., Schmitz, S., Veigel,C. and Mansson, A. “Drug Effect Unveils Inter-head Cooperativity and Strain-dependent ADP Release in Fast Skeletal Actomyosin” J. Biol. Chem. (2009), 384, 22926-22937.


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Last edited: 05/12/2017 03:57:00