Search Results - "Visser, N.V"

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  1. 1

    Structural Changes of Yellow Cameleon Domains Observed by Quantitative FRET Analysis and Polarized Fluorescence Correlation Spectroscopy by Borst, J.W., Laptenok, S.P., Westphal, A.H., Kühnemuth, R., Hornen, H., Visser, N.V., Kalinin, S., Aker, J., van Hoek, A., Seidel, C.A.M., Visser, A.J.W.G.

    Published in Biophysical journal (01-12-2008)
    “…Förster resonance energy transfer (FRET) is a widely used method for monitoring interactions between or within biological macromolecules conjugated with…”
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  2. 2

    5-Fluorotryptophan as dual probe for ground-state heterogeneity and excited-state dynamics in apoflavodoxin by 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.

    Published in FEBS letters (03-09-2009)
    “…The apoflavodoxin protein from Azotobacter vinelandii harboring three tryptophan (Trp) residues, was biosynthetically labeled with 5-fluorotryptophan (5-FTrp)…”
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    Green-Fluorescent Protein from the Bioluminescent Jellyfish Clytia gregaria Is an Obligate Dimer and Does Not Form a Stable Complex with the Ca2+-Discharged Photoprotein Clytin by Malikova, Natalia P, Visser, Nina V, van Hoek, Arie, Skakun, Victor V, Vysotski, Eugene S, Lee, John, Visser, Antonie J. W. G

    Published in Biochemistry (Easton) (24-05-2011)
    “…Green-fluorescent protein (GFP) is the origin of the green bioluminescence color exhibited by several marine hydrozoans and anthozoans. The mechanism is…”
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  5. 5

    Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs by Visser, A. J. W. G, Laptenok, S. P, Visser, N. V, van Hoek, A, Birch, D. J. S, Brochon, J.-C, Borst, J. W

    Published in European biophysics journal (2010)
    “…Förster resonance energy transfer (FRET) is a powerful method for obtaining information about small-scale lengths between biomacromolecules. Visible…”
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  6. 6

    A general approach for detecting folding intermediates from staedy-state and time-resolved fluorescence of single-tryptophan-containing proteins by Laptenok, S, Visser, N.V, Ruchira, A, Westphal, A.H, Hoek, A., van, Mierlo, C.P.M., van, Stokkum, I.H.M., van, Amerongen, H., van, Visser, A.J.W.G

    Published in Biochemistry (Easton) (2011)
    “…During denaturant-induced equilibrium (un)folding of wild-type apoflavodoxin from Azotobacter vinelandii, a molten globule-like folding intermediate is formed…”
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  7. 7

    Tryptophan-Tryptophan Energy Migration as a Tool to Follow Apoflavodoxin Folding by Visser, Nina V., Westphal, Adrie H., van Hoek, Arie, van Mierlo, Carlo P.M., Visser, Antonie J.W.G., van Amerongen, Herbert

    Published in Biophysical journal (01-09-2008)
    “…Submolecular details of Azotobacter vinelandii apoflavodoxin (apoFD) (un)folding are revealed by time-resolved fluorescence anisotropy using wild-type protein…”
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  8. 8

    Oxidation of unsaturated phospholipids in membrane bilayer mixtures is accompanied by membrane fluidity changes by Borst, Jan Willem, Visser, Nina V, Kouptsova, Olga, Visser, Antonie J.W.G

    Published in Biochimica et biophysica acta (24-08-2000)
    “…Steady-state and time-resolved fluorescence spectroscopy has been used to obtain information on oxidation processes and associated dynamical and structural…”
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  9. 9

    Fluorescence dynamics of staphylococcal nuclease in aqueous solution and reversed micelles by Visser, A J, van Engelen, J, Visser, N V, van Hoek, A, Hilhorst, R, Freedman, R B

    Published in Biochimica et biophysica acta (16-02-1994)
    “…The dynamical fluorescence properties of the sole tryptophan residue (Trp-140) in Staphylococcus aureus nuclease (EC 3.1.31.1) have been investigated in…”
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  10. 10

    Circular dichroism spectroscopy of fluorescent proteins by Visser, Nina V, Hink, Mark A, Borst, Jan Willem, van der Krogt, Gerard N.M, Visser, Antonie J.W.G

    Published in FEBS letters (19-06-2002)
    “…Circular dichroism (CD) spectra have been obtained from several variants of green fluorescent protein: blue fluorescent protein (BFP), enhanced cyan…”
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  11. 11

    Practical use of corrected fluorescence excitation and emission spectra of fluorescent proteins in Förster Resonance Energy Transfer (FRET) studies by Hink, M.A, Visser, N.V, Borst, J.W, Hoek, A., van, Visser, A.J.W.G

    Published in Journal of fluorescence (01-03-2003)
    “…Corrected fluorescence excitation and emission spectra have been obtained from several enhanced variants of the green fluorescent protein (EGFP) isolated from…”
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  12. 12

    Direct observation of resonance tryptophan-to-chromophore energy transfer in visible fluorescent proteins by Visser, Nina V., Borst, Jan Willem, Hink, Mark A., van Hoek, Arie, Visser, Antonie J.W.G.

    Published in Biophysical chemistry (01-08-2005)
    “…Visible fluorescent proteins from Aequorea victoria contain next to the fluorophoric group a single tryptophan residue. Both molecules form a single…”
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  13. 13

    Molecular dynamics of monopyrenyl lipids in liposomes from global analysis of time-resolved fluorescence of pyrene monomer and excimer emission by Novikov, E.G, Visser, N.V, Malevitskaia, V.G, Borst, J.W, Hoek, A., van, Visser, A.J.W.G

    Published in Langmuir (2000)
    “…The diffusion coefficients of 1-palmitoyl-2-(pyrenodecanoyl)-sn-glycero-3-phosphocholine (pyr10PC) in different bilayer membranes are determined from global…”
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  14. 14
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    Antigen–antibody interactions: binding studies with fluorescence and surface plasmon resonance exemplified by acid-traseolide as antigen by Visser, N.V, Smit-Kingma, I.E

    “…The interaction between the musk fragrance acid-traseolide and monoclonal antibodies (mAB) generated against this odorant has been investigated with two…”
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  16. 16

    Time-Resolved Fluorescence Investigations of the Interaction of the Voltage-Sensitive Probe RH421 with Lipid Membranes and Proteins by Visser, Nina V, van Hoek, Arie, Visser, Antonie J. W. G, Frank, Joachim, Apell, Hans-Juergen, Clarke, Ronald J

    Published in Biochemistry (Easton) (19-09-1995)
    “…Fluorescence lifetimes and fluorescence anisotropy decays of the voltage-sensitive styryl-pyridinium dye RH421 have been measured in the presence of…”
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  17. 17
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    Time-Resolved Fluorescence Study of the Dissociation of FMN from the Yellow Fluorescence Protein from Vibrio fischeri by Visser, Antonie J. W. G., van Hoek, Arie, Visser, Nina V., Lee, Yongho, Ghisla, Sandro

    Published in Photochemistry and photobiology (01-03-1997)
    “…Time-resolved fluorescence spectroscopy of the flavin mononucleotide (FMN) prosthetic group of the yellow fluorescence protein (YFP) from Vibrio fischeri has…”
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    Fluorescence analysis of the Hansenula polymorpha peroxisomal targeting signal‐1 receptor, Pex5p by Boteva, Raina, Koek, Anne, Visser, Nina V., Visser, Antonie J.W.G., Krieger, Elmar, Zlateva, Theodora, Veenhuis, Marten, van der Klei, Ida

    Published in European journal of biochemistry (01-11-2003)
    “…Correct sorting of newly synthesized peroxisomal matrix proteins is dependent on a peroxisomal targeting signal (PTS). So far two PTSs are known. PTS1 consists…”
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