Publications

1. van Mierlo, C.P.M., Vervoort, J. & Müller, F. in Flavins and Flavoproteins 1987 (Edmondson, D.E.
     & McCormick, D.B. eds.), pp. 271-274, Walter de Gruyter & Co., Berlin-New York.
    "Two-dimensional NMR studies on Megasphaera elsdenii flavodoxin".

2. Mülller, F., Vervoort, J., van Mierlo, C.P.M., Mayhew, S.G., van Berkel, W.J.H. & Bacher, A.
    in Flavins and Flavoproteins 1987 (Edmondson, D.E. & McCormick, D.B. eds.), pp. 261-270,
    Walter de Gruyter & Co., Berlin-New York.
    "C-13, N-15 and Two-dimensional NMR techniques in Flavoprotein Research".

3. van Mierlo, C.P.M., Vervoort, J., Mülller, F. & Bacher, A. (1990) Eur. J. Biochem. 187, 521-541.
     "A two-dimensional 1H NMR study on Megasphaera elsdenii flavodoxin in the reduced
    state: sequential assignments".

4. van Mierlo, C.P.M., Mülller, F. & Vervoort, J. (1990) Eur. J. Biochem. 189, 589- 600.
    "Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced
    state as determined by two-dimensional 1H NMR".

5. van Mierlo, C.P.M., Lijnzaad, P., Vervoort, J., Mülller, F., Berendsen, H.J.C. & de Vlieg, J.
    (1990) Eur. J. Biochem. 194, 185-198.
    "Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications,
    as determined by two-dimensional 1H NMR and restrained molecular dynamics".

6. van Mierlo, C.P.M., van der Sanden, B.P.J., van Woensel, P., Mülller, F. & Vervoort, J. (1990) Eur.
    J. Biochem. 194, 199-216.
    "A two- dimensional 1H NMR study on Megasphaera elsdenii flavodoxin in the oxidized state
    and some comparisons with the two-electron reduced state".

7. van Mierlo, C.P.M. (1990). Thesis (Wageningen University, The Netherlands), pp. 1-220
    (Copies available on request).
    "Proton NMR studies on Megasphaera elsdenii flavodoxin: structure elucidation by 2D- NMR and
    implications".

8. Vervoort, J., van Mierlo, C.P.M. & Legall, J. in Flavins and Flavoproteins 1990 (Curti, B., Ronchi
    S. & Zanetti G. eds.), pp. 361-368, Walter de Gruyter & Co., Berlin-New York.
    "Two-dimensional NMR studies of Desulfovibrio vulgaris and Megasphaera elsdenii flavodoxin".

9. Darby, N.J., van Mierlo, C.P.M. & Creighton, T.E. (1990) FEBS Lett. 279, 61- 64.
    "The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor".

10. van Mierlo, C.P.M., Vervoort, J., Mülller, F. & Veeger, C. (1991) in New Trends in
    Biological Chemistry (Ozawa, T., ed.), pp. 33-46, Japan Sci. Soc. Press, Tokyo/Springer-
    Verlag, (Berlin).
    "Two-dimensional 1H-NMR studies on two-electron reduced Megasphaera elsdenii flavodoxin".

11. Wijmenga, S.S. & van Mierlo, C.P.M. (1991) Eur. J. Biochem. 195, 807- 822.
    "Three-dimensional correlated NMR study of Megasphaera elsdenii flavodoxin in the oxidized state".

12. van der Graaf, M., van Mierlo, C.P.M. & Hemminga, M.A. (1991) Biochemistry 30, 5722-5727.
    "Solution conformation of a peptide fragment representing a proposed RNA-binding site of a
    viral coat protein studied by two-dimensional NMR".

13. van Mierlo, C.P.M., Darby, N.J., Neuhaus, D. & Creighton, T.E. (1991) J. Mol. Biol. 222, 353-371.
    "(14-38, 30-51) Double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor:
    a two-dimensional 1H nuclear magnetic resonance study".

14. van Mierlo, C.P.M., Darby, N.J., Neuhaus, D. & Creighton, T.E. (1991) J. Mol. Biol. 222, 373-390.
    "Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding
    intermediate of bovine pancreatic trypsin inhibitor".

15. Darby, N.J., van Mierlo, C.P.M., Scott, G.H.E., Neuhaus, D. & Creighton, T.E. (1992)
    J. Mol. Biol. 224, 905-911.
    "Kinetic roles and conformational properties of the non-native two-disulphide intermediates in
    the refolding of bovine pancreatic trypsin inhibitor".

16. van Mierlo, C.P.M., Darby, N.J. & Creighton, T.E. (1992) Proc. Natl. Acad. Sci. USA
    89, 6775-6779.
    "The partially folded conformation of the Cys30-Cys51 intermediate in the disulphide
    folding pathway of bovine pancreatic trypsin inhibitor".

17. Neuhaus, D. & van Mierlo, C.P.M. (1992) J. Magn. Reson. 100, 221-228.
    "Measurement of heteronuclear NOE enhancement factors in biological macromolecules.
    A convenient pulse sequence for use with aqueous solutions".

18. van Mierlo, C.P.M., Darby, N.J., Keeler, J., Neuhaus, D. & Creighton, T.E. (1993) J. Mol. Biol.
    229, 1125-1146.
    "Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway
    of bovine pancreatic trypsin inhibitor: 1H and 15N resonance assignments and determination
    of backbone dynamics from 15N relaxation measurements".

19. Kemmink, J., van Mierlo, C.P.M., Scheek, R.M. & Creighton, T.E. (1993) J. Mol.
    Biol. 230, 312-322.
    "Local structure due to an aromatic-amide interaction observed by 1H-nuclear magnetic
    resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin
    inhibitor".

20. Darby, N.J., van Mierlo, C.P.M. & Creighton, T.E. (1993) in Innovations on proteases and
    inhibitors, (F.X. Avilés, ed.), pp. 391-406, Walter de Gruyter, Berlin.
    "BPTI as a model protein for understanding protein folding pathways".

21. van Mierlo, C.P.M., Kemmink, J., Neuhaus, D., Darby, N.J. & Creighton, T.E. (1994)
    J. Mol. Biol. 235, 1044-1061.
    "1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30- 51,5-14)
    and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor".

22. Steensma, E., Heering, H.A., Hagen, W.R. & van Mierlo, C.P.M. (1996) Eur. J. Biochem.
    235, 167-172.
    "Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II
    as measured by cyclic voltammetry and EPR spectroscopy".

23. Wijmenga, S.S., van Mierlo, C.P.M. & Steensma, E. (1996) J. Biomol. NMR 8, 319-330.
    "Doubly sensitivity enhanced 3D TOCSY-HSQC".

24. Steensma, E., Heering, H.A., Hagen, F. & van Mierlo, C.P.M. (1996) in Dynamics and the
    problem of recognition in biological macromolecules (O. Jardetzky & J-F. Lefèvre eds.),
    pp. 293-294, Plenum Press, New York and London.
    "Comparison of wild-type, C70A and C70S Azotobacter vinelandii flavodoxin -
    backbone assignments and secondary structure of oxidized C70A flavodoxin as determined
    by three-dimensional heteronuclear NMR spectroscopy".

25. van Mierlo, C.P.M., Steensma, E., van Dongen, W.M.A.M. & van Berkel, W.J.H. in Flavins
    and Flavoproteins 1996 (Stevenson, K.J., Massey, V. & Williams, Jr., C.H. eds.),
    pp. 449-452, University of Calgary Press, Calgary, Alberta, Canada.
    "NMR studies on apoflavodoxin II from Azotobacter vinelandii".

26. Wijmenga, S.S., Steensma, E. & van Mierlo, C.P.M. (1997) J. Magn. Reson. 124, 459-467.
    "Doubly sensitivity-enhanced 3D HCCH-TOCSY of 13C- labeled proteins in H2O
    using heteronuclear cross polarization and pulsed field gradients".

27. Steensma, E., Nijman, M.J.M., Bollen, Y.J.M., de Jager, P.A., van den Berg, W.A.M., van
    Dongen, W.M.A.M. & van Mierlo, C.P.M. (1998) Protein Science 7, 306-317.
    "Apparant local stability of the secondary structure of Azotobacter vinelandii holo- flavodoxin I
    as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding".

28. Steensma, E. & van Mierlo, C.P.M. (1998) J. Mol. Biol. 282, 653-666.
    "Structural characterisation of apoflavodoxin shows that the location of the most stable
    nucleus differs among proteins with a flavodoxin-like topology".

29. van Mierlo, C.P.M., van Dongen, W.M.A.M., Vergeldt, F., van Berkel, W.J.H. &
    Steensma, E. (1998) Protein Science 7, 2331-2344.
    "The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively
    stable folding intermediate".

30. van Mierlo, C.P.M. & Steensma, E. (1999) Journal of Molecular Catalysis B: Enzymatic 7,
    147-156 (Special issue based on the First International Conference on Protein Stabilisation
    "Enzyme stabilisation, methods and applications", Leeds, UK, 1998).
    "Stabilisation centres differ between structurally homologous proteins as shown by
    NMR spectroscopy".

31. van Mierlo, C.P.M., de Jongh, H.H.J. & A.J.W.G. Visser (2000) in Physical Chemistry of

    Biological Interfaces (Baszkin, A. & Norde, W. eds.), Marcel Dekker Inc., New York, USA,
    p. 673- 709.
    "Circular Dichroism of proteins in solutions and at interfaces".

32. van Mierlo, C.P.M., van den Oever, J.M.P. & Steensma, E. (2000) Protein Science 9, 145-157.
    "Apoflavodoxin (un)folding followed at the residue-level by NMR".

33. van Mierlo, C.P.M. & Steensma, E. (2000) Journal of Biotechnology 79, 281- 298
    (special issue based on the Second International Symposium on Industrial Proteins "Problems
    and potential of denaturation of proteins for industrial use").
    "Protein folding and stability investigated by fluorescence, CD, and NMR spectroscopy.
    The flavodoxin story".

34. van Mierlo, C.P.M., de Jongh, H.H.J. & Visser A.J.W.G. (2000) in Applied Spectroscopy
    Reviews 35(4), 277 - 313.
    "Circular Dichroism of proteins in solutions and at interfaces".

35. Engel, M.F.M., van Mierlo, C.P.M., & Visser A.J.W.G. (2000) in Biophysical Journal
    78, 910.
    "Conformational changes of proteins at solid/water interfaces".

36. van Mierlo, C.P.M., van den Oever, J.M.P., & Steensma, E. (2001) in Nova Acta Leopoldina
    Supplementum 16, 63 - 64.
    "Apoflavodoxin (un)folding followed at the residue-level by NMR".

37. Engel, M.F.M., van Mierlo, C.P.M., & Visser, A.J.W.G. (2002) in J. Biol. Chem.
    277, 10922 - 10930.
    "Kinetic and structural characterisation of adsorption induced unfolding of bovine alpha-lactalbumin".

38. Hengeveld, A.F., van Mierlo, C.P.M., van den Hooven, H.W., Visser, A.J.W.G. & de Kok, A.
    (2002) in Biochemistry 41, 7490 - 7500.
    "Functional and structural characterisation of a synthetic peptide representing the N-terminal
    domain of prokaryotic pyruvate dehydrogenase".

39. Engel, M.F.M., Visser, A.J.W.G. & van Mierlo, C.P.M. (2003) in Biophysical Journal
    84(2), 1643-Pos.
    "Adsorption induced unfolding of bovine alpha-lactalbumin".

40. Engel, M.F.M., Visser, A.J.W.G. & van Mierlo, C.P.M. (2003) in Langmuir
    19, 2929 - 2937.
    "Refolding of adsorbed bovine alpha-lactalbumin during surfactant induced displacement
    from a hydrophobic interface".

41. Arnaudov, L.N., de Vries, R., Ippel, H. & van Mierlo, C.P.M. (2003) in Biomacromolecules
    4, 1614 - 1622.
    "Multiple steps during the formation of beta- lactoglobulin fibrils".

42. Ippel, J.H., Pouvreau, L., Kroef, T., Gruppen, H., Versteeg, G., van den Putten, P., Struik, P.C.
    & van Mierlo, C.P.M. (2004) in Proteomics 4, 226 - 234.
    "In vivo uniform 15N-isotope labelling of plants: Using the greenhouse for structural proteomics".

43. Engel, M.F.M., Visser, A.J.W.G. & van Mierlo, C.P.M. (2004) in Langmuir 20, 5530 - 5538.
    "Adsorption of bovine alpha-lactalbumin on solid nanospheres and its subsequent displacement
    studied by NMR spectroscopy".

44. Bollen, Y.J.M., Sanchéz, I.E. & van Mierlo, C.P.M. (2004) in Biochemistry 43, 10475 - 10489.
    "Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii
    apoflavodoxin".

45. Engel, M.F.M., Visser, A.J.W.G. & van Mierlo, C.P.M. (2004) in Proc. Natl. Acad. Sci. USA
    101(31), 11316 - 11321.
    "Conformation and orientation of a protein folding intermediate trapped by adsorption".

46. Bollen, Y.J.M., Nabuurs, S.M., van Berkel, W.J.H. & van Mierlo, C.P.M. (2005) in J. Biol. Chem.
    280(9), 7836 - 7844.
    "Last in, first out: the role of cofactor binding in flavodoxin folding".

47. Bollen, Y.J.M. & van Mierlo, C.P.M. (2005) in Biophysical Chemistry 114, 181 - 189.
    "Protein topology affects the appearance of intermediates during the folding of proteins with a
    flavodoxin-like fold".

48. Alagaratnam, S., van Pouderoyen, G., Pijning, T., Dijkstra, B.W., Cavazzini, D., Rossi, G.L.,
    van Dongen, W.M.A.M., van Mierlo, C.P.M., van Berkel, W.J.H. & Canters, G.W. (2005) in
    Protein Sci. 14, 2284 - 2295.
    "A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: structural
    determinants of redox potential".

49. Bollen, Y.J.M., Kamphuis, M.B. & van Mierlo, C.P.M. (2006) in Proc. Natl. Acad. Sci. USA

    103(11), 4095 - 4100.
    "The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals
    non-productive misfolded intermediates".

50. Duarte, A.M.S., Wolfs, C.J.A.M., van Nuland, N.A.J., Harrison, M.A., Findlay, J.B.C.,
    van Mierlo, C.P.M. & Hemminga, M.A. (2007) in Biochimica et Biophysica Acta - Biomembranes
    1768, 218 - 227.
    "Structure and localization of an essential transmembrane segment of the proton
    translocation channel of yeast H+-V-ATPase".

51. Duarte, A.M.S., de Jong, E.R., Wechselberger, R., van Mierlo, C.P.M. & Hemminga, M.A. (2007)
    in Biochimica et Biophysica Acta - Biomembranes 1768, 2263 - 2270.
    "Segment TM7 from the cytoplasmic hemi-channel from V0-H+-V-ATPase includes a flexible region"
    that has a potential role in proton translocation".

52. Duarte, A.M.S., van Mierlo, C.P.M. & Hemminga, M.A. (2008) in J. Phys. Chem. B
    112, 8664 - 8671.
    "Molecular dynamics study of the solvation of an alpha-helical transmembrane peptide by DMSO".

53. Visser, N.V., Westphal, A.H., van Hoek, A., van Mierlo, C.P.M., Visser, A.J.W.G.,
    & van Amerongen, H. (2008) in Biophys. J. 95(5), 2462 - 2469.
    "Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding".

54. Engel, R., Westphal, A.H., Huberts, D.H.E.W., Nabuurs, S.M., Lindhoud, S., Visser, A.J.W.G., &
    van Mierlo, C.P.M. (2008) in J. Biol. Chem. 283(41), 27383 - 27394.
    "Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of
    the off-pathway intermediate during apoflavodoxin folding".

55. Nabuurs, S.M., Westphal, A.H., & van Mierlo, C.P.M. (2008) in J. Am. Chem. Soc. 130, 16914 - 16920.
    "Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due
    to docking of (non)native structure elements in unfolded molecules".

56. Nabuurs, S.M. Westphal, A.H., & van Mierlo, C.P.M. (2009) in J. Am. Chem. Soc.
    131, 2739 - 2746.
    "Non-cooperative formation of the off-pathway molten-globule during the folding of the
    alpha-beta parallel protein apoflavodoxin".

57. Nabuurs, S.M. Westphal, A.H., & van Mierlo, C.P.M. (2009) in J. Am. Chem. Soc.
    131, 8290 - 8295.
    "Topological switching between an alpha-beta parallel protein and a remarkably helical molten globule".

58. Visser, N.V. Westphal, A.H., Nabuurs, S.M., van Hoek, A., van Mierlo, C.P.M., Visser, A.J.W.G., Broos, J.,
    & van Amerongen, H. (2009) in FEBS Lett. 583, 2785 - 2788.
    "5-Fluorotryptophan as dual probe for ground-state heterogeneity and excited state
    dynamics in apoflavodoxin".

59. Ippel, J.H., Koutsopoulos, S., Nabuurs, S.M., van Berkel, W.J.H., van der Oost, J. & van Mierlo, C.P.M. (2010)
    in Biochem. Biophys. Res. Commun. 391, 370 - 375.
    "NMR characterization of a 264-residue hyperthermostable endo-beta-1,3-glucanase".

60. Nabuurs, S.M. & van Mierlo, C.P.M. (2010) in J. Biol. Chem. 285, 4165 - 4172.
    "Interrupted hydrogen/deuterium exchange reveals the stable core of the remarkably helical molten globule of
    alpha-beta parallel protein flavodoxin".

61. Nabuurs, S.M., de Kort, B.J., Westphal, A.H. & van Mierlo, C.P.M. (2010) in Eur. Biophys. J. 39, 689 - 698.
    "Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement".

62. Laptenok, S.P., Visser, N.V., Engel, R., Westphal, A.H., van Hoek, A., van Mierlo, C.P.M., van Stokkum, I.H.M.,
    van Amerongen, H. & Visser, A.J.W.G. (2011) in Biochemistry 50, 3441 - 3450.
    "A general approach to detect folding intermediates from steady-state and time-resolved fluorescence
    of single tryptophan-containing proteins".

63. Lindhoud, S., van den Berg, W.A.M., van den Heuvel, R.H.H., Heck, A.J.R., van Mierlo, C.P.M.
   & van Berkel, W.J.H. (2012) in PLoS ONE 7(7), e41363 (doi:10.1371/journal.pone.0041363).
    "Cofactor binding protects flavodoxin against oxidative stress".

64. Bollen, Y.J.M., Westphal, A.H., Lindhoud, S., van Berkel, W.J.H. & van Mierlo, C.P.M. (2012)
    in Nature Communications 3:1010, doi: 10.1038/ncomms2010.
    "Distant residues mediate picomolar-binding affinity of a protein cofactor".