{ "id": "epd9e2xjda", "slug": "microscale-thermophoresis", "title": "Microscale thermophoresis", "updated": "2026-10-25", "topic_path": [ { "id": "life", "label": "Life and health", "api_url": "https://www.edgepedia.org/api/v1/topics/life" }, { "id": "life.biology", "label": "Biological foundations", "api_url": "https://www.edgepedia.org/api/v1/topics/life.biology" }, { "id": "life.biology.biochemistry", "label": "Biochemistry and metabolism", "api_url": "https://www.edgepedia.org/api/v1/topics/life.biology.biochemistry" }, { "id": "life.biology.biochemistry.practice", "label": "Biochemistry field and methods", "api_url": "https://www.edgepedia.org/api/v1/topics/life.biology.biochemistry.practice" }, { "id": "life.biology.biochemistry.practice.methods", "label": "Biochemical methods and techniques", "api_url": "https://www.edgepedia.org/api/v1/topics/life.biology.biochemistry.practice.methods" }, { "id": "life.biology.biochemistry.practice.methods.assays", "label": "Assay techniques", "api_url": "https://www.edgepedia.org/api/v1/topics/life.biology.biochemistry.practice.methods.assays" } ], "geo": [ { "id": "geo.nongeo.t2001.life.biology", "label": "Non-geographic · 2001 to 2020: Biological foundations", "api_url": "https://www.edgepedia.org/api/v1/geo/geo.nongeo.t2001.life.biology", "path": [ { "id": "geo.nongeo", "label": "Non-geographic", "api_url": "https://www.edgepedia.org/api/v1/geo/geo.nongeo" }, { "id": "geo.nongeo.t2001", "label": "Non-geographic · 2001 to 2020", "api_url": "https://www.edgepedia.org/api/v1/geo/geo.nongeo.t2001" }, { "id": "geo.nongeo.t2001.life", "label": "Life and health", "api_url": "https://www.edgepedia.org/api/v1/geo/geo.nongeo.t2001.life" }, { "id": "geo.nongeo.t2001.life.biology", "label": "Biological foundations", "api_url": "https://www.edgepedia.org/api/v1/geo/geo.nongeo.t2001.life.biology" } ] } ], "excerpt": "Microscale thermophoresis (MST) is an optical biophysical method that measures biomolecular binding in free solution by moving fluorescently labeled molecules in a laser-induced temperature gradient, yielding affinities in about 10 minutes without surface immobilization.", "snippet": "Microscale thermophoresis (MST) is an optical biophysical method that measures biomolecular binding in free solution by moving fluorescently labeled molecules in a laser-induced temperature gradient, yielding affinities in about 10 minutes without surface immobilization.", "node": "life.biology.biochemistry.practice.methods.assays", "markdown": "# Microscale thermophoresis\n\nMicroscale thermophoresis (MST) is an all-optical, free-solution biophysical method that quantifies biomolecular binding by monitoring the movement of fluorescently labeled molecules in a microscopic temperature gradient and fitting the resulting titration curve to a binding model to yield a dissociation constant (\\( K_{\\mathrm{d}} \\)).[1](https://www.nature.com/articles/ncomms1093) A typical assay keeps one fluorescent partner at a constant low concentration, titrates the unlabeled partner, and reads out binding from changes in normalized fluorescence; affinities from nanomolar to millimolar are reported in a single assay format, in low-microliter volumes, and in complex matrices such as serum and cell lysate.[2](https://nanotempertech.com/mst/) Because both heating and detection are optical, no surface immobilization is involved, and an equilibrium affinity is determined in about 10 minutes in free solution.[3](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf)\n\n| Key fact | Detail |\n|---|---|\n| Measured quantity | Change in normalized fluorescence (\\( F_{\\mathrm{norm}} \\)) during laser-induced thermophoresis, fitted to the law of mass action to give \\( K_{\\mathrm{d}} \\)[1](https://www.nature.com/articles/ncomms1093) |\n| Heating | 1480 nm infrared laser, steady-state temperature increase of typically 2–6 K[1](https://www.nature.com/articles/ncomms1093) |\n| Sample use | About 4 µL per capillary, 16-capillary titration, roughly 192 µL per triplicate experiment[4](https://beta.iopscience.iop.org/article/10.1088/2050-6120/ac82a6) |\n| Affinity range | 1 nM–500 mM on the Monolith NT.115; pM–mM claims appear in other guides[5](https://biotech.ug.edu.pl/sites/default/files/_nodes/strona-biotechnologia/73064/files/monolith_manual.pdf) |\n| Timescale | Equilibrium \\( K_{\\mathrm{d}} \\) in about 10 min; a full trace cycle lasts about 20 s[3](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf) • [4](https://beta.iopscience.iop.org/article/10.1088/2050-6120/ac82a6) |\n| Matrices | Buffer, serum, cell lysate, detergents, liposomes, nanodiscs[2](https://nanotempertech.com/mst/) |\n| Main noise source | Sample aggregates; adsorption to capillary walls is the other common failure mode[3](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf) |\n\n## How it works\n\nMST exploits thermophoresis, the directed movement of particles in a temperature gradient, also known as the Ludwig–Soret effect.[6](https://doi.org/10.1016/j.ymeth.2012.12.005) An infrared laser at 1480 nm is coupled into the fluorescence excitation and emission path and focused into the sample, producing a steady-state temperature increase of typically 2–6 K after about 150 ms on a microscopic length scale; the introducing paper describes a roughly 25 µm distribution in ~500 nl fused-silica capillaries, while later reviews describe a heated volume of ~50 µm diameter.[1](https://www.nature.com/articles/ncomms1093) • [7](https://www.sciencedirect.com/science/article/pii/S0022286014002750) At this scale the measurement avoids artifacts from thermal convection, which was the key advance of the fluorescence microfluidic imaging technique underlying MST.[8](https://doi.org/10.1073/pnas.0603873103)\n\nIn steady state the thermophoretic flow is counterbalanced by mass diffusion, so the local depletion follows the Soret relation \\( c_{\\mathrm{hot}}/c_{\\mathrm{cold}} = \\exp(-S_{T} \\cdot \\Delta T) \\), where \\( S_{T} \\) is the Soret coefficient and \\( \\Delta T \\) the temperature rise.[6](https://doi.org/10.1016/j.ymeth.2012.12.005) • [3](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf) Duhr and Braun's solvation-entropy theory states, in simple terms, that the Soret coefficient equals the negative solvation entropy of the particle–solvent system divided by \\( k \\cdot T \\), and predicts thermodiffusion of DNA and polystyrene beads with about 20% average accuracy.[8](https://doi.org/10.1073/pnas.0603873103) Binding changes a molecule's surface area, hydration shell, and effective charge, which is why even ion or small-molecule binding alters the thermophoretic signal.[1](https://www.nature.com/articles/ncomms1093) The normalized fluorescence follows \\( F_{\\mathrm{norm}} = 1 + (\\partial F/\\partial T - S_{T}) \\cdot \\Delta T \\), combining the intrinsic temperature dependence of fluorescence with thermophoretic depletion.[3](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf)\n\nThe MST trace contains two superimposed components: an immediate fluorescence change when the laser turns on, the TRIC (temperature-related intensity change) component, caused by the temperature dependence of fluorophore quantum yield, and the slower thermophoretic movement over the following seconds.[2](https://nanotempertech.com/mst/) The trace is divided into five regions: initial fluorescence, T-jump (several 100 ms), thermophoresis (several seconds), inverse T-jump, and back-diffusion after the laser is switched off.[6](https://doi.org/10.1016/j.ymeth.2012.12.005) The T-jump reflects the local dye environment and can respond to ligands binding nearby, whereas thermophoresis depends on the properties of the whole molecule or complex; either or both regions can yield a \\( K_{\\mathrm{d}} \\).[7](https://www.sciencedirect.com/science/article/pii/S0022286014002750) In current best practice the hot region is defined as 0.5–1.5 s after the T-jump, and when binding changes fluorescence by more than 20% of the absolute signal, the initial fluorescence is analyzed instead of the TRIC signal.[9](https://link.springer.com/article/10.1007/s00249-021-01532-6)\n\n## How it is done\n\nThe standard workflow starts with fluorescent labeling of one partner, usually the larger one, using NHS-ester chemistry on primary amines with the protein adjusted to 2–20 µM during labeling.[1](https://www.nature.com/articles/ncomms1093) Free dye must be removed, for example by dialysis or desalting, because free dye shows both temperature-jump and thermophoresis signals.[10](https://www.sciencedirect.com/science/article/abs/pii/S0003269717303986) Capillaries come in standard treated, hydrophilic-coated, and hydrophobic-coated types (K002, K004, K003) to suppress nonspecific adsorption to the glass.[11](https://www.isbg.fr/wp-content/uploads/2016/03/MST-Starting-guide.pdf)\n\nThe titration is a 1:1 dilution series of 16 ligand concentrations starting about 20-fold above the expected \\( K_{\\mathrm{d}} \\), with at least three points in the baseline and saturation regions; only 4 µL fills a capillary, but working volumes should not fall below 20 µL.[11](https://www.isbg.fr/wp-content/uploads/2016/03/MST-Starting-guide.pdf) The labeled molecule is used at a low concentration, at or below the expected \\( K_{\\mathrm{d}} \\), with the instrument manual stating typically 1–10 nM.[5](https://biotech.ug.edu.pl/sites/default/files/_nodes/strona-biotechnologia/73064/files/monolith_manual.pdf) [Fluorescence](https://www.edgepedia.org/fluorescence) is adjusted to 200–1,500 counts by varying concentration or LED power, and quality rules require a signal amplitude above 5 response units, baseline noise at least threefold lower than the amplitude, and initial fluorescence variation within ±10%.[11](https://www.isbg.fr/wp-content/uploads/2016/03/MST-Starting-guide.pdf) The software computes \\( F_{\\mathrm{norm}} \\) as the ratio of fluorescence after a given laser-on time (\\( F_{1} \\)) to fluorescence before laser activation (\\( F_{0} \\)), and the \\( K_{\\mathrm{d}} \\) is obtained by fitting \\( F_{\\mathrm{norm}} \\) versus ligand concentration to the law of mass action.[5](https://biotech.ug.edu.pl/sites/default/files/_nodes/strona-biotechnologia/73064/files/monolith_manual.pdf)\n\n## Origin\n\nThermophoresis was observed, and subsequent research focused mostly on inorganic molecules and polymer blends until biomolecule measurements were developed.[3](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf) • [1](https://www.nature.com/articles/ncomms1093) The theoretical foundation came from Stefan Duhr and [Dieter Braun](https://www.edgepedia.org/dieter-braun)'s 2006 PNAS paper on why molecules move along a temperature gradient.[8](https://doi.org/10.1073/pnas.0603873103) MST as a protein-binding assay in biological liquids was reported by Christoph J. Wienken, Philipp Baaske, Ulrich Rothbauer, Dieter Braun, and Stefan Duhr in [Nature Communications](https://www.edgepedia.org/nature-communications) in 2010.[1](https://www.nature.com/articles/ncomms1093) The introducing paper credits earlier biomolecule thermophoresis measurements by Braun and Libchaber and by Piazza, and prior work showing that thermophoresis could analyze DNA aptamer interactions with thrombin and ATP.[1](https://www.nature.com/articles/ncomms1093)\n\nMethod extensions followed quickly: Karina Zillner and colleagues described MST for protein:nucleic acid interactions in 2011,[12](https://doi.org/10.1007/978-1-61779-424-7_18) Susanne A. I. Seidel and colleagues introduced label-free MST using intrinsic tryptophan fluorescence in 2012,[13](https://doi.org/10.1002/anie.201204268) and Seidel and colleagues published a methods paper the same year on MST under previously challenging conditions such as membrane proteins and cell lysate.[6](https://doi.org/10.1016/j.ymeth.2012.12.005) Duhr and Baaske founded the LMU spin-out NanoTemper Technologies GmbH, and the Monolith was introduced as a commercial instrument in 2011.[1](https://www.nature.com/articles/ncomms1093) • [9](https://link.springer.com/article/10.1007/s00249-021-01532-6) Pawel Linke and colleagues reported an automated MST screening approach for fragment-based lead discovery in 2015.[14](https://doi.org/10.1177/1087057115618347)\n\n## Variants\n\nThe Monolith NT.115 uses blue, green, and red LED excitation sets (blue 460–490 nm for fluorescein, AlexaFluor488, and GFP; red 600–650 nm for AlexaFluor647, NT647, and Cy5).[6](https://doi.org/10.1016/j.ymeth.2012.12.005) • [15](https://cmi.hms.harvard.edu/microscale-thermophoresis) The NT.115Pico detects low picomolar concentrations of red fluorophores, enabling \\( K_{\\mathrm{d}} \\) determination in the low pM range.[7](https://www.sciencedirect.com/science/article/pii/S0022286014002750) The NT.LabelFree variant excites intrinsic tryptophan fluorescence at 280 nm with emission at 360 nm, removing the need for a tag, but it is unsuitable for serum or cell lysate because of high background UV fluorescence, and many protein–protein interactions cannot be measured label-free because aromatic residues interfere.[4](https://beta.iopscience.iop.org/article/10.1088/2050-6120/ac82a6) The NT.Automated screens 96 samples in 30 minutes.[16](https://lab.research.sickkids.ca/sbc-facility/wp-content/uploads/sites/40/2021/03/Monolith_MST_General-Introduction-and-Application-Note.pdf)\n\nNanoTemper reserves the term MST for the capillary-based Monolith and uses TRIC for the plate-based Dianthus, which combines spectral shift and TRIC in 384- and 1536-well formats.[9](https://link.springer.com/article/10.1007/s00249-021-01532-6) • [17](https://link.springer.com/article/10.1007/s12551-025-01359-x) The MonolithX has added spectral shift technology to the Monolith line, and the Monolith Omni combines four technologies: spectral shift, TRIC, nanoTAK (kinetics from a rapid temperature step), and nanoLISA (thermal unfolding up to 95 °C).[17](https://link.springer.com/article/10.1007/s12551-025-01359-x) • [18](https://nanotempertech.com/wp-content/uploads/2026/06/NT-Monolith-Omni-Data-File_2026.pdf) Outside the commercial ecosystem, Shibin Mao and colleagues implemented a CMOS detector-array MST platform with full-field imaging, validated against SPR for protein–protein and micromolar protein–small molecule interactions.[19](https://doi.org/10.1063/5.0293380)\n\n## Applications\n\nPublished applications span protein–small molecule, protein–protein, protein–DNA and protein–RNA, antibody–antigen, and membrane-protein binding, including measurements in liposomes, nanodiscs, and detergents.[7](https://www.sciencedirect.com/science/article/pii/S0022286014002750) • [20](https://pmc.ncbi.nlm.nih.gov/articles/PMC3846881/) Example values from the introducing paper: human interferon-γ binding to a specific antibody gave \\( K_{\\mathrm{d}} = 10 \\pm 2 \\) nM in buffer and 165 ± 26 nM in crude E. coli lysate; calmodulin bound \\( \\mathrm{Ca}^{2+} \\) with \\( K_{\\mathrm{d}} = 2.8 \\pm 0.2 \\) µM, with no binding observed for \\( \\mathrm{Mg}^{2+} \\); and the kinase inhibitor quercetin bound PKA with \\( K_{\\mathrm{d}} = 130 \\pm 30 \\) nM in buffer, about 400-fold weaker in human serum.[1](https://www.nature.com/articles/ncomms1093) Seidel and colleagues quantified Grb2 dimerization, synaptotagmin-1 binding to PIP2 liposomes, and neurotensin receptor 1 binding at \\( K_{\\mathrm{d}} \\leq 20 \\) nM label-free.[6](https://doi.org/10.1016/j.ymeth.2012.12.005) GFP-fusion proteins in unpurified cell lysates have been used to determine transcription factor–oligonucleotide affinities.[20](https://pmc.ncbi.nlm.nih.gov/articles/PMC3846881/)\n\n## Limitations and alternatives\n\nThe main noise source is poor sample quality, especially aggregates; adsorption to capillary walls is countered by polymer-coated capillaries or additives such as Tween-20, BSA, or DTT.[3](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf) • [7](https://www.sciencedirect.com/science/article/pii/S0022286014002750) Core-facility guidance adds 0.05% Tween-20 or another detergent to prevent capillary sticking and 0.5–1 mg/mL BSA to reduce nonspecific binding.[15](https://cmi.hms.harvard.edu/microscale-thermophoresis) Ligand-induced fluorescence quenching must be distinguished from material loss, for example with an SD-test (4% SDS, 40 mM DTT, 5 min at 95 °C); thermophoresis can also be drastically and unpredictably affected by high concentrations of a protein titrant.[11](https://www.isbg.fr/wp-content/uploads/2016/03/MST-Starting-guide.pdf) • [10](https://www.sciencedirect.com/science/article/abs/pii/S0003269717303986) Because the labeled partner is held well below \\( K_{\\mathrm{d}} \\), stoichiometry is not readily available, and only two analysis models, 1:1 and Hill, were in wide use as of 2017, neither serving 1:2 curves well.[10](https://www.sciencedirect.com/science/article/abs/pii/S0003269717303986) MST provides no kinetic rate constants, no binding-site or stoichiometry information without complementary NMR or crystallography, and has a working temperature range of 20–45 °C.[21](https://www.xantec.com/material/pdf/comparison_of_biomolecular_interaction_techniques.pdf) • [4](https://beta.iopscience.iop.org/article/10.1088/2050-6120/ac82a6) • [22](https://www.mdpi.com/1422-0067/23/14/7672)\n\nCompared with ITC and SPR, MST avoids surface immobilization and consumes far less sample, and it works in virtually any buffer including plasma and lysate.[7](https://www.sciencedirect.com/science/article/pii/S0022286014002750) A benchmark study by 32 European and two US groups on 40 Monolith instruments found good agreement for the lysozyme–NAG3 interaction, with MST-derived \\( K_{\\mathrm{d}} \\) of about 4 µM (label-free) against ITC values of 6.5–8.5 µM; the same study attributes MST's limited acceptance among biophysicists to incompletely understood signal contributions and licensing to a single instrument developer.[9](https://link.springer.com/article/10.1007/s00249-021-01532-6)\n\n## References\n\n1. [Protein-binding assays in biological liquids using microscale thermophoresis (Wienken, Baaske, Rothbauer, Braun, Duhr; Nature Communications 2010, 1, 100)](https://www.nature.com/articles/ncomms1093)\n2. [MicroScale thermophoresis (MST), NanoTemper Technologies (manufacturer)](https://nanotempertech.com/mst/)\n3. [Molecular Interaction Studies Using Microscale Thermophoresis (Jerabek-Willemsen (Duhr) et al.; Assay and Drug Development Technologies 2011, 9(4):342–53)](https://www.uni-hohenheim.de/fileadmin/einrichtungen/mst/Duhr_et_al.pdf)\n4. [Microscale thermophoresis as a powerful growing analytical technique for the investigation of biomolecular interaction and the determination of binding parameters (Biophysical Reviews, 2022)](https://beta.iopscience.iop.org/article/10.1088/2050-6120/ac82a6)\n5. [User Manual Monolith NT.115 (NanoTemper)](https://biotech.ug.edu.pl/sites/default/files/_nodes/strona-biotechnologia/73064/files/monolith_manual.pdf)\n6. [Susanne A.I. Seidel and colleagues (2012). Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions. Methods.](https://doi.org/10.1016/j.ymeth.2012.12.005)\n7. [MicroScale Thermophoresis: Interaction analysis and beyond (Jerabek-Willemsen et al.; J. Mol. Struct. 2014, 1077, 101–113)](https://www.sciencedirect.com/science/article/pii/S0022286014002750)\n8. [Stefan Duhr, Dieter Braun (2006). Why molecules move along a temperature gradient. Proceedings of the National Academy of Sciences.](https://doi.org/10.1073/pnas.0603873103)\n9. [Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study (Eur. Biophys. J. 2021)](https://link.springer.com/article/10.1007/s00249-021-01532-6)\n10. [Using two-site binding models to analyze microscale thermophoresis data (Scheuermann et al., Analytical Biochemistry, 2017)](https://www.sciencedirect.com/science/article/abs/pii/S0003269717303986)\n11. [User Starting Guide Monolith NT.115 (NanoTemper)](https://www.isbg.fr/wp-content/uploads/2016/03/MST-Starting-guide.pdf)\n12. [Karina Zillner and colleagues (2011). Microscale Thermophoresis as a Sensitive Method to Quantify Protein: Nucleic Acid Interactions in Solution. Methods in molecular biology.](https://doi.org/10.1007/978-1-61779-424-7_18)\n13. [Susanne A. I. Seidel and colleagues (2012). Label‐Free Microscale Thermophoresis Discriminates Sites and Affinity of Protein–Ligand Binding. Angewandte Chemie International Edition.](https://doi.org/10.1002/anie.201204268)\n14. [Pawel Linke and colleagues (2015). An Automated Microscale Thermophoresis Screening Approach for Fragment-Based Lead Discovery. SLAS DISCOVERY.](https://doi.org/10.1177/1087057115618347)\n15. [MicroScale Thermophoresis (MST) | Center for Macromolecular Interactions, Harvard Medical School](https://cmi.hms.harvard.edu/microscale-thermophoresis)\n16. [NanoTemper Monolith NT.Automated for MST (Hospital for Sick Children SBC Facility)](https://lab.research.sickkids.ca/sbc-facility/wp-content/uploads/sites/40/2021/03/Monolith_MST_General-Introduction-and-Application-Note.pdf)\n17. [High-throughput investigation of macromolecular interactions for drug development using spectral shift technology (Biophysical Reviews, 2025)](https://link.springer.com/article/10.1007/s12551-025-01359-x)\n18. [Monolith Omni Data File (NanoTemper, 2026)](https://nanotempertech.com/wp-content/uploads/2026/06/NT-Monolith-Omni-Data-File_2026.pdf)\n19. [Shibin Mao and colleagues (2026). Design and implementation of a microscale thermophoresis system based on complementary metal–oxide–semiconductor (CMOS) detector array. Review of Scientific Instruments.](https://doi.org/10.1063/5.0293380)\n20. [Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis (PMC)](https://pmc.ncbi.nlm.nih.gov/articles/PMC3846881/)\n21. [Comparison of Biomolecular Interaction Techniques (XanTec white paper)](https://www.xantec.com/material/pdf/comparison_of_biomolecular_interaction_techniques.pdf)\n22. [Microscale Thermophoresis as a Tool to Study Protein Interactions and Their Implication in Human Diseases (Int. J. Mol. Sci. 2022, 23, 7672)](https://www.mdpi.com/1422-0067/23/14/7672)\n\n---\n*Topic: Encyclopedia › Life and health › Biological foundations › Biochemistry and metabolism › Biochemistry field and methods › Biochemical methods and techniques › Assay techniques*\n\n*Initially written Sep 29, 2026 · Reviewed: Sep 30, 2026 · Edited: Oct 15, 2026; Oct 25, 2026 · Last review: Sep 30, 2026*\n\n*Copyright 2026 EdgeChat AI, a subsidiary of Biostate AI.*\n\nLicense: Edgepedia Community License 1.0, https://www.edgepedia.org/edgepedia/license\n", "same_as": [], "url": "https://www.edgepedia.org/microscale-thermophoresis", "markdown_url": "https://www.edgepedia.org/microscale-thermophoresis.md", "license": { "name": "Edgepedia Community License 1.0", "url": "https://www.edgepedia.org/edgepedia/license", "summary": "Free with credit, commercial use included. AI training is open to everyone. For other uses, organizations over USD 100M in revenue or 100M monthly users license separately.", "spdx": "LicenseRef-Edgepedia-Community-1.0" }, "credit": "\"Microscale thermophoresis\", Edgepedia (EdgeChat), https://www.edgepedia.org/microscale-thermophoresis. Edgepedia Community License 1.0.", "credit_md": "\"[Microscale thermophoresis](https://www.edgepedia.org/microscale-thermophoresis)\", Edgepedia (EdgeChat), [https://www.edgepedia.org/microscale-thermophoresis](https://www.edgepedia.org/microscale-thermophoresis). [Edgepedia Community License 1.0](https://www.edgepedia.org/edgepedia/license).", "credit_html": "\"Microscale thermophoresis\", Edgepedia (EdgeChat), https://www.edgepedia.org/microscale-thermophoresis. Edgepedia Community License 1.0.", "speakable": "Microscale thermophoresis is an optical biophysical method that measures biomolecular binding in free solution by moving fluorescently labeled molecules in a laser-induced temperature gradient, yielding affinities in about 10 minutes without surface immobilization." }