One-Cuvette Sample Compartment
Overview of K2
The K2 family of frequency-domain spectrometers provides researchers with a solid, well-proven instrumentation platform for the most demanding fluorescence and phosphorescence applications.
With installed units all over the world, the K2 family of multifrequency, cross-correlation phase and modulation spectrometers represents a solid and well-proven approach to fluorescence and phosphorescence instrumentation for the research laboratory. K2 is used by researchers at ETH in Zurich, Switzerland, MIT in Cambridge, MA, NIH in Rockville, MD, and at the NASA research facility in Huntsville, AL.
Its optical design and automatic instrument control are state-of-the-art for steady-state and time-resolved fluorescence measurements. Full automation and the user-friendly Vinci software package make the instrument easy to use for both the student and the scientist.
Key Features of K2
- Lifetime measurement capabilities from 1 millisecond to 1 picosecond
- Complete lifetime scans in less than one minute on routine samples with proprietary FastScan technology
- A compact footprint and a short optical pathlength for maximum sensitivity and efficient light coupling into the sample
- T-format and parallel beam optical design for fast and precise polarization measurements
- Full automation of all instrument components (cuvette holder, polarizers, shutters, filterwheel, monochromators, and stirrers)
- PC-controlled integration of temperature bath, titrator, stopped-flow apparatus and pressure pump
- Measurement of fast kinetics data with one millisecond resolution in photon counting mode
- 80 MHz pre-amplifier discriminators delivering linearity up to over eight million counts per second on each channel
- Flexible instrument configuration
- Upgradeable with Ti:Sapphire laser and laser diodes
Fully Automated and Upgradeable Models of K2
K2-001 with K2 FastScan
The FastScan is our most popular model: lifetime data acquisition on a routine sample can be acquired in less than one minute using either a lamp or a laser. The cross-correlation is user-selectable up to 5,000Hz and data acquisition is performed through a FFT routine; the instrument covers the modulation frequency range from 300KHz up to 350MHz with a lamp and up to 450MHz using a cw laser.
K2-002 1.2GHz Upgrade
This model requires a mode-locked laser as excitation source and a microchannel plate detector (MCP-PMT) for the collection of fluorescence. Alternatively, a laser diode can be utilized as the light source to measure frequency responses up to about 1GHz. The cross-correlation is user-selectable up to 5,000Hz and data acquisition is performed through a FFT routine. It includes the FastScan upgrade and operates at modulation frequency up to 1.2GHz.
K2-003 6GHz Upgrade
The K2-003 is an upgrade of the K2-002: it operates in the frequency range up to 6GHz.
Product Specifications for K2
Measurements (Steady-State Fluorescence)
- Corrected excitation and emission spectra
- Excitation-emission matrices
- Polarization (anisotropy) measurements
- Millisecond kinetics in photon counting mode
- Dual-wavelength-ratiometric excitation or emission measurements
Measurements (Time-Resolved Fluorescence)
- Multiple decay times from millisecond to picosecond time scale Anisotropy decays Phase- and modulation-resolved spectra (up to 3 components in a mixture) Time-resolved spectra
Light Sources
- 300 W xenon arc lamp, 45 mW/nm brightness at 275 nm Laser diodes Light emitting diodes (LEDs) Continuous wave lasers (argon-ion, krypton-ion, helium-cadmium) Mode-locked lasers (Ti:Sapphire) Synchrotron light beams
Monochromators
- Single concave holographic grating Wavelength range: from 200 nm to 1200 nm (dependent on selected grating)
Detectors
- Selected side-on photomultiplier tubes in room-temperature or cooled housing (for frequency response up to 800 MHz) Microchannel plate detectors (for frequency response > 800 MHz) Optional: CCD camera
Detection Modes
- Photon counting electronics, 10 KHz, on 3 independent channels Analog Output on 3 channels
Frequency-Response
- From DC up to 10 GHz
Frequency Synthesizers
- Marconi Instruments Programmed Test Sources Gigatronics Hewlett Packard
Light Modulation
- Wide aperture Pockels cell (for lamp and cw lasers) up to 350 MHz Direct modulation (for laser diodes and LEDs) up to 700 MHz Harmonic content of pulsed sources up to 10 GHz
Polarizers
- UV-grade Glan-Thompson, 10x10 mm, L/A=2.0 UV-grade Glan-Thompson, 14x14 mm, L/A=2.0 UV-grade Glan-Taylor, 10x10 mm, L/A=2.0 (for high power lasers)
Pre-Amplifier Discriminators
- 100 MHz bandwidth, TTL output
Focusing and Collection Geometry
- Parallel beam design for precise polarization measurements
Dynamic Range
- Linear up to 4 million counts/second
Wavelength Accuracy
- ±0.2 nm
Wavelength Reproducibility
- ±0.25 nm
Slew Rate
- 160 nm/s (optional double grating)
Lifetime Measurements Range
- From 100 milliseconds to 20 picoseconds (depending upon the model; the shortest measurable decay time is determined by the light detectors frequency response)
Operating System
- Windows 11
Power Requirements
- Universal power input: 110-240 V, 50/60 Hz, 400 VAC
Dimensions
- 885 mm (L) x 600 mm (W) x 330 mm (H)
Weight (kg)
- 45
Example Configuration for K2
Product Accessories for K2
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Two-Cuvette Sample Compartment
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Three-Cuvette Sample Compartment
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Variable-Angle, Front Surface Sample Compartment
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Total Internal Reflection Fluorescence (TIRF) Flow Cell
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Absorption Measurements Accessory
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High-Pressure Cell System
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Microwell Plate Reader
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Integrating Sphere
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Dewar Flask
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Cryostat
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Fiber Optics
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Single Syringe Titrator
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Double Syringe Titrator
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Polarizers
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Stopped-Flow Packages for ISS Spectrofluorimeters
Product Software for K2
Vinci
A comprehensive multidimensional fluorescence spectroscopy software program designed to enhance the capabilities and performance of ISS spectrofluorometers.
Learn MoreProduct Resources
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Anisotropy Decay Measurements
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Fluorescence Basic Instrumentation
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Fluorescence Lifetime
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Fluorescence Polarization
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Fluorescence Spectroscopy
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Long-Wavelength Polarization Standards
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Measurement of Fluorescence Quantum Yields on ISS Instrumentation Using Vinci
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Polarization Measurements: Parallel vs. Non-Parallel Beam Geometry
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Phasor Plots for the Analysis of Time-resolved Fluorescence
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What is Total Internal Reflection Fluorescence (TIRF)?
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A Critical Comparison of Xenon Lamps
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“A Fluorescence Spectroscopy Study on the Interactions of the TAT-PTD Peptide with Model Lipid Membranes.” Tiriveedhi, V., Butko, P. Biochemistry, 2007, 46, 3888-3895.
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“A New Competitive Fluorescence Assay for the Detection of Patulin Toxin.” de Champdoré, M., Bazzicalupo, P., De Napoli, L., Montesarchio, D., Di Fabio, G., Cocozza, I., Parracino, A., Rossi, M., D'Auria, S. Anal. Chem., 2007, 79, 751-757.
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“IIAGlc Inhibition of Glycerol Kinase: A Communications Network Tunes Protein Motions at the Allosteric Site.” Yu, P., Lasagna, M., Pawlyk, A.C., Reinhart, G.D., Pettigrew, D.W. Biochemistry, 2007, Printing Pending.
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“Structural Characterization of Novel Chitin-Binding Lectins from the GenusArtocarpus and Their Antifungal Activity.” Trindade, M.B., Lopes, J.L.S., Soares-Costa, A., Monteiro-Moreira, A.C., Moreira, R.A., Oliva, M.L.V., Beltramini, L.M. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 2006, 1764(1), 146-152.
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“Inhibition of Amyloid Fibril Formation and Cytotoxicity by Hydroxyindole Derivatives.” Cohen, T., Frydman-Marom, A., Rechter, M., Gazit, E. Biochemistry, 2006, 45, 4727-4735.
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“Structural Dynamics of the Actin–Myosin Interface by Site-Directed Spectroscopy.” Korman, V.L., Anderson, S.E.B., Prochniewicz, E., Titus, M.A., Thomas, D.D. Journal of Molecular Biology, 2006, 356(5), 1107-1117.
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“Genetic and Fluorescence Studies of Affinity Maturation in Related Antibodies.” Pauyo, T., Hilinski, G.J., Chiu, P.T., Hansen, D.E., Choi, Y.J., Ratner, D.I., Shah-Mahoney, N., Southern, C.A., O'Hara, P.B. Molecular Immunology, 2006, 43(7), 812-821.
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“Expression and Physicochemical Characterization of an Extracellular Segment of the Receptor Protein Tyrosine Phosphatase IA-2.” Primo, M.E., Sica, M.P., Risso, V.A., Poskus, E., Ermácora, M.R. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 2006, 1764(2), 174-181.
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“Phosphorylation of a Single Head of Smooth Muscle Myosin Activates the Whole Molecule.” Rovner, A.S., Fagnant, P.M., Trybus, K.M. Biochemistry, 2006, 45, 5280-5289.
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“Complex Formation Between Plasmid DNA and Self-Aggregates of Deoxycholic Acid-Modified Chitosan.” Lee, K.Y., Kwon, I.C., Jo, W.H., Jeong, S.Y. Polymer, 2005, 46(19), 8107-8112.
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“Phospholamban Pentamer Quaternary Conformation Determined by In-Gel Fluorescence Anisotropy.” Robia, S.L., Flohr, N.C., Thomas, D.D. Biochemistry, 2005, 44(11), 4302-4311.
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“Essential Role for Pro21 in Phospholamban for Optimal Inhibition of the Ca-ATPase.” Li, J., Boschek, C.B., Xiong, Y., Sacksteder, C.A., Squier, T.C., Bigelow, D.J. Biochemistry, 2005, 44(49), 16181-16191.
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“Structural Uncoupling between Opposing Domains of Oxidized Calmodulin Underlies the Enhanced Binding Affinity and Inhibition of the Plasma Membrane Ca-ATPase.” Chen, B., Mayer, M.U., Squier, T.C. Biochemistry, 2005, 44(12), 4737-4747.
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“A Detergent-like Mechanism of Action of the Cytolytic Toxin Cyt1A fromBacillus thuringiensis var.israelensis.” Manceva, S.D., Pusztai-Carey, M., Russo, P.S., Butko, P. Biochemistry, 2005, 44(2), 589-597.
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“Dynamic Motion of Helix A in the Amino-Terminal Domain of Calmodulin Is Stabilized upon Calcium Activation.” Chen, B., Mayer, M.U., Markillie, L.M., Stenoien, D.L., Squier, T.C. Biochemistry, 2005, 44(3), 905-914.
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“Interaction of the 20 kDa and 63 kDa Fragments of Anthrax Protective Antigen: Kinetics and Thermodynamics.” Christensen, K.A., Krantz, B.A., Melnyk, R.A., Collier, R.J. Biochemistry, 2005, 44(3), 1047-1053.
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“Trans Fatty Acid Derived Phospholipids Show Increased Membrane Cholesterol and Reduced Receptor Activation as Compared To Their Cis Analogs.” Niu, S.-L., Mitchell, D.C., Litman, B.J. Biochemistry, 2005, 44(11), 4458-4465.
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“Ethanol-Perturbed Amyloidogenic Self-Assembly of Insulin: Looking for Origins of Amyloid Strains.” Dzwolak, W., Grudzielanek, S., Smirnovas, V., Ravindra, R., Nicolini, C., Jansen, R., Loksztejn, A., Porowski, S., Winter, R. Biochemistry, 2005, 44(25), 8948-8958.
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“Improved "Optical Highlighter" Probes Derived from Discosoma Red Fluorescent Protein.” Robinson, L.C. Biophys. J., 2005, 88, 1444-1457.
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“Sequence-Specific Fluorescence Detection of DNA by Polyamide-Thiazole Orange Conjugates.” Fechter, E.J., Olenyuk, B., Dervan, P.B. J. Am. Chem. Soc., 2005, 127(47), 16685-16691.
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“Heterologous Expression, Characterization and Structural Studies of a Hydrophobic Peptide from the HIV-1 p24 Protein.” Castilho, P.V., Campana, P.T., Garcia, A.F., Beltramini, L.M., Araújo, A.P.U. Peptides, 2005, 26(2), 243-249.
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“Direct Detection of Calmodulin Tuning By Ryanodine Receptor Channel Targets Using a Ca2+-Sensitive Acrylodan-Labeled Calmodulin.” Fruen, B.R., Balog, E.M., Schafer, J., Nitu, F.R., Thomas, D.D., and Corena, R.L. Biochemistry, 2005, 44, 278-284.
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“A Nature of Conformational Changes of Yeast tRNAPhe: High Hydrostatic Pressure Effects.” Giel-Pietraszuk, M., Barciszewski, J. International Journal of Biological Macromolecules, 2005, 37(3), 109-114.
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“Probing the Interior of Peptide Amphiphile Supramolecular Aggregates.” Tovar, J.D., Claussen, R.C., Stupp, S.I. J. Am. Chem. Soc., 2005, 127(20), 7337-7345.
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“Reductive and Oxidative DNA Damage by Photoactive Platinum(II) Intercalators.” Lu, W., Vicic, D.A., Barton, J.K. Inorg. Chem., 2005, 44(22), 7970-7980.
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“Oligomeric State and Mode of Self-Association ofThermotoga maritima Ribosomal Stalk Protein L12 in Solution.” Moens, P.D.J., Wahl, M.C., Jameson, D.M. Biochemistry, 2005, 44(9), 3298-3305.
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“Conformation of a Synthetic Antigenic Peptide from HIV-1 p24 Protein Induced by Ionic Micelles.” Campana, P.T., Beltramini, L.M., Costa-Filho, A.J., Tonarelli, G., Lottersberger, J., Bianconi, M.L. Biophysical Chemistry, 2005, 113(2), 175-182.
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“A Recombinant Glutamine-Binding Protein fromEscherichia coli: Effect of Ligand-Binding on Protein Conformational Dynamics.” Herman, P., Vecer, J., Scognamiglio, V., Staiano, M., Rossi, M., D'Auria, S. Biotechnol. Prog., 2004, 20(6), 1847-1854.
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“Cloning and Characterization of the cDNA for the Brazilian Cratomorphus distinctus Larval Firefly Luciferase: Similarities with European Lampyris noctiluca and Asiatic Pyrocoelia luciferases.” Viviani, V.R., Arnoldi, F.G.C., Brochetto-Braga, M., Ohmiya, Y. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2004, 139(2), 151-156.
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“Conformational Changes within the Cytosolic Portion of Phospholamban upon Release of Ca-ATPase Inhibition.” Li, J., Bigelow, D. J., Squier, T. C. Biochemistry, 2004, 43(13), 3870-3879.
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“Effects of Ethanol on Lipid Bilayers with and without Cholesterol: The Distearoylphosphatidylcholine System.” Tran, R., Ho, S., Dea, P. Biophysical Chemistry, 2004, 110(1-2), 39-47.
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“Conformational and Enzymatic Changes of 20S Proteasome of Rat Natural Killer Cells Induced by Mono- and Divalent Cations.” Reshetnyak, Y.K., Kitson, R.P., Lu, M., Goldfarb, R.H. Journal of Structural Biology, 2004, 145(3), 263-271.
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“High Hydrostatic Pressure Perturbs the Interactions between CF0F1 Subunits and Induces a Dual Effect on Activity.” Souza, M.O., Creczynski-Pasa, T.B., Scofano, H.M., Gräber, P., Mignaco, J.A. The International Journal of Biochemistry & Cell Biology, 2004, 36(5), 920-930.
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“Phospholamban Binds in a Compact and Ordered Conformation to the Ca-ATPase.” Li, J., Xiong, Y., Bigelow, D. J., Squier, T. C. Biochemistry, 2004, 43(2), 455-463.
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“DNA Charge Transport: Conformationally Gated Hopping through Stacked Domains.” O'Neill, M. A., Barton, J. K. J. Am. Chem. Soc., 2004, 126(37), 11471-11483.
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“Cholesterol Superlattice Modulates the Activity of Cholesterol Oxidase in Lipid Membranes.” Wang, M. M., Olsher, M., Sugar, I. P., Chong, P. L.-G. Biochemistry, 2004, 43(8), 2159-2166.
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“Characterization of Lecithin: Cholesterol Acyltransferase Expressed in a Human Lung Cell Line.” Lane, S.B., Tchedre, K.T., Nair, M.P., Thigpen, A.E., Lacko, A.G. Protein Expression and Purification, 2004, 36(2), 157-164.
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“Correlation between Mechanical and Enzymatic Events in Contracting Skeletal Muscle Fiber.” Shepard, A., Borejdo, J. Biochemistry, 2004, 43(10), 2804-2811.
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“Direct Detection of Phospholamban and Sarcoplasmic Reticulum Ca-ATPase Interaction in Membranes Using Fluorescence Resonance Energy Transfer.” Mueller, B., Karim, C. B., Negrashov, I. V., Kutchai, H., Thomas, D. D. Biochemistry, 2004, 43(27), 8754-8765.
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“Partitioning of Dual-Lipidated Peptides into Membrane Microdomains: Lipid Sorting vs Peptide Aggregation.” Janosch, S., Nicolini, C., Ludolph, B., Peters, C., Volkert, M., Hazlet, T. L., Gratton, E., Waldmann, H., Winter, R. J. Am. Chem. Soc., 2004, 126(24), 7496-7503.
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“Calcium Activation of the Ca-ATPase Enhances Conformational Heterogeneity between Nucleotide Binding and Phosphorylation Domains.” Chen, B., Squier, T. C., Bigelow, D. J. Biochemistry, 2004, 43(14), 4366-4374.
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“Quantification of Allosteric Influence of Escherichia coli Phosphofructokinase by Frequency Domain Fluorescence.” Pham, A.S., Reinharty, G.D. Biophys. J., 2003, 85, 656-666.
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“Evidence for Tryptophan Residues in the Cation Transport Path of the Na+,K+-ATPase.” Yudowski, G. A., Bar Shimon, M., Tal, D. M., Gonzalez-Lebrero, R. M., Rossi, R. C., Garrahan, P. J., Beauge, L. A., Karlish, S. J. D. Biochemistry, 2003, 42(34), 10212-10222.
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“Phosphorylation by cAMP-Dependent Protein Kinase Modulates the Structural Coupling between the Transmembrane and Cytosolic Domains of Phospholamban.” Li, J., Bigelow, D. J., Squier, T. C. Biochemistry, 2003, 42(36), 10674-10682.
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“Fluorescence Resonance Energy Transfer Studies on Anthrax Lethal Toxin.” Croney, J.C., Cunningham, K.M., Collier, R.J., Jameson, D.M. FEBS Letters, 2003, 550, 175-178.
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“Surface Changes and Role of Buried Water Molecules during the Sulfane Sulfur Transfer in Rhodanese and Azotobacter vinelandii: A Fluorescence Quenching and Nuclear Magnetic Relaxation Dispersion Spectroscopic Study.” Fasano, M., Orsale, M., Melino, S., Nicolai, E., Forlani, F., Rosato, N., Cicero, D., Pagani, S., Paci, M. Biochemistry, 2003, 42, 8550-8557.
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“Sequence Specific Fluorescence Detection of Double Strand DNA.” Rucker, V.C., Foister, S., Melander, C., Dervan, P.B. J. Am. Chem. Soc., 2003, 125(5), 1195-1202.
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“Structural and Biochemical Characterization of a Fluorogenic Rhodamine-Labeled Malarial Protease Substrate.” Blackman, M.J., Corrie, J.E., Croney, J.C., Kelly, G., Eccleston, J.F., Jameson, D.M. Biochemistry, 2002, 41, 12244-12252.
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“DNA Cross-Linking with Metallointercalator-Peptide Conjugates.” Copeland, K.D., Lueras, A.M.K., Stemp, E.D.A., Barton, J.K. Biochemistry, 2002, 41, 12785-12797.
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“Lateral Diffusion Coefficients in Membranes Measured by Resonance Energy Transfer and a New Algorithm for Diffusion in Two Dimensions.” Kuśba, J., Li, L., Gryczynski, I., Piszczek, G., Johnson, M., Lakowicz, J.R. Biophys. J., 2002, 82, 1358-1372.
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“Low Temperature and Pressure Stability of Picornaviruses: Implications for Virus Uncoating.” Oliveira, A.C., Ishimaru, D., Gonçalves, R.B., Smith, T.J., Mason, P., Sá-Carvalho, D., Silva, J.L. Biophys. J., 1999, 76, 1270-1279.
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“Hg2+ Reacts with Different Components of the NADPH: Protochlorophyllide Oxidoreductase Macrodomains.” Solymosi, K., Lenti, K., Myśliwa-Kurdziel, B., Fidy, J., Strzalka, K., Böddi, B. Plant Biology, 2004, 6, 358-367.
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“Real-Time Determination of Picomolar Free Cu(II) in Seawater Using a Fluorescence-Based Fiber Optic Biosensor.” Zeng, H.-H., Thompson, R.B., Maliwal, B.P., Fones, G. R., Moffett, J.W., Fierke, C.A. Anal. Chem., 2003, 75(24), 6807-6812.
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“Fabrication and Characterization of Planar Plasmonic Substrates with High Fluorescence Enhancement.” Szmacinski, H., Bedugu, R., Lakowicz, J.R.. J. Phys. Chem., 2010, 114(49), 21142-21149.
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“Physicochemical Characterizations of Self-Assembled Nanoparticles of Glycol Chitosan-Deoxycholic Acid Conjugates.” Kim, K., Kwon, S., Park, J.H., Chung, H., Jeong, S.Y., Kwon, I.C., Kim, I.-S. Biomacromolecules, 2005, 6(2), 1154-1158.
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“Thermosensitive Poly(organophosphazene) Hydrogels for a Controlled Drug Delivery.” Kang, G.D., Cheon, S.H., Khang, G., Song, S.-C. European Journal of Pharmaceutics and Biopharmaceutics, in press, Available online 9 March 2006.
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“Polycations Enhance Emulsion-Mediated in Vitro and in Vivo Transfection.” Kim, T.W., Chung, H., Kwon, I.C., Sung, H.C., Shin, B.C., Jeon, S.Y. International Journal of Pharmaceutics, 2005, 295(1-2), 35-45.
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“PsbS-Dependent Enhancement of Feedback De-Excitation Protects Photosystem II from Photoinhibition.” Li, X., Muller-Moule, P., Gilmore, A.M., Niyogi, K. PNAS, 2002, 99, 15222-15227.
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“Daunomycin Binding to Detergent Micelles: A Model System for Evaluating the Hydrophobic Contribution to Drug-DNA Interactions.” Dignam, J.D., Qu, X., Ren, J., Chaires, J.B. J. Phys. Chem. B, 2007, 111(39), 11576-11584.
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“Synthesis, Characterization and Fluorescence Study of Eu(III) Tungstates and Molybdates.” De Farias, R.F, Airoldi, C., Belian, M.F., Alvres, Jr., S. Journal of Alloys and Compounds, 2006, 419(1-2), 50-53.
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“Preparative Routes to Luminescent Mixed-Ligand Rhenium(I) Dicarbonyl Complexes.” Smithback, J.L., Helms, J.B., Schutte, E., Woessner, S.M., Sullivan, B.P. Inorg. Chem., 2006, 45(5), 2163-2174.
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“Detection of Adsorption of Ru(II) and Os(II) Polypyridyl Complexes on Gold and Silver Nanoparticles by Single-Photon Counting Emission Measurements.” Glomm, W.R., Moses, S.J., Brennaman, M.K., Papanikolas, J.M., Franzen, S. J. Phys. Chem. B, 2005, 109(2), 804-810.
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“Synthesis and Micellar Characteristics of Dendron-PEG Conjugates.” Chang, Y., Park, C., Kim, K.T., Kim, C. Langmuir, 2005, 21(10), 4334-4339.
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“Determination of Diffusion Coefficients of Humic Substances by Fluorescence Correlation Spectroscopy: Role of Solution Conditions.” Lead, J.R., Starchev, K., Wilkinson, K.J. Environ. Sci. Technol., 2003, 37(3), 482-487.
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“Nanosecond Photoreduction of Cytochrome P450cam by Channel-Specific Ru-diimine Electron Tunneling Wires.” Dunn, A.R., Dmochowski, I.J., Winkler, J.R., Gray, H.B. J. Am. Chem. Soc., 2003, 125(41), 12450-12456.
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“Long Wavelength Fluorescence Lifetime Standards for Front-Face Fluorometry.” McCranor, B.J., Thompson, R.B. J. Fluoresc., March 2010, 20(2), 435-440.
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“Modeling of Spherical Fluorescent Glucose Microsensor Systems: Design of Enzymatic Smart Tattoos.” Brown, J.Q., McShane, M.J. Biosens. Bioelectron., 2006, 21(9), 1760-9.
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“Coordinatively Induced Length Control and Photoluminescence of W18O49 Nanorods.” Woo, K., Hong, J., Ahn, J.-P., Park, J.-K., Kim, K.-J. Inorg. Chem., 2005, 44(20), 7171-7174.
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“Fatty Acid Sensor for Low-Cost Lifetime-Assisted Ratiometric Sensing Using a Fluorescent Fatty Acid Binding Protein.” Bartolome, A., Bardliving, C., Rao, G., Tolosa, L. Analytical Biochemistry, 2005, 345(1), 133-139.
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“Short-lived fluorescence component of DPH reports on lipid–water interface of biological membranes.” Konopásek, I., Vecer, J., Strzalka, K., Amler, E. Chemistry and Physics of Lipids, 2004, 130(2) 135-144.
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“[Ru(bpy)2(L)]Cl2: Luminescent Metal Complexes That Bind DNA Base Mismatches.” Ruba, E., Hart, J. R., Barton, J. K. Inorg. Chem., 2004, 43(15), 4570-4578.
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“Reorientational Dynamics of Enzymes Adsorbed on Quartz: A Temperature-Dependent Time-Resolved TIRF Anisotropy Study.” Czeslik, C., Royer, C., Hazlett, T., Mantulin, W. Biophysical Journal, 2003, 84(4), 2533-2541.
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“Synthesis and Characterization of a Sulfhydryl-Reactive Rhenium Metal-Ligand Complex.” Dattelbaum, J.D., Abugo, O.O., Lakowicz, J.R. Bioconjug. Chem., 2000, 11(4), 533-536.
