LOPEZ-MENDEZ, Blanca, Bruno BARON, Chad A BRAUTIGAM, Thomas A JOWITT, Stefan H KNAUER, Stephan UEBEL, Mark A WILLIAMS, Arthur SEDIVY, Olga ABIAN, Celeste ABREU, Malgorzata ADAMCZYK, Wojciech BAL, Sylvie BERGER, Alexander K BUELL, Carlo CAROLIS, Tina DAVITER, Alexander FISH, Maria GARCIA-ALAI, Christian GUENTHER, Josef HAMACEK, Jitka HOLKOVÁ, Josef HOUSER, Chris JOHNSON, Sharon KELLY, Andrew LEECH, Caroline MAS, Daumantas MATULIS, Stephen H MCLAUGHLIN, Roland MONTSERRET, Rouba NASREDDINE, Reine NEHME, Quyen NGUYEN, David ORTEGA-ALARCON, Kathryn PEREZ, Katja PIRC, Grzegorz PISZCZEK, Marjetka PODOBNIK, Natalia RODRIGO, Jasmina ROKOV-PLAVEC, Susanne SCHAEFER, Tim SHARPE, June SOUTHALL, David STAUNTON, Pedro TAVARES, Ondrej VANEK, Michael WEYAND and Di WU. Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study. European Biophysics Journal With Biophysics Letters. NEW YORK: SPRINGER, 2021, vol. 50, 3-4, p. 411-427. ISSN 0175-7571. Available from: https://dx.doi.org/10.1007/s00249-021-01532-6.
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Basic information
Original name Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study
Authors LOPEZ-MENDEZ, Blanca, Bruno BARON, Chad A BRAUTIGAM, Thomas A JOWITT, Stefan H KNAUER, Stephan UEBEL, Mark A WILLIAMS, Arthur SEDIVY, Olga ABIAN, Celeste ABREU, Malgorzata ADAMCZYK, Wojciech BAL, Sylvie BERGER, Alexander K BUELL, Carlo CAROLIS, Tina DAVITER, Alexander FISH, Maria GARCIA-ALAI, Christian GUENTHER, Josef HAMACEK, Jitka HOLKOVÁ (203 Czech Republic, belonging to the institution), Josef HOUSER (203 Czech Republic, belonging to the institution), Chris JOHNSON, Sharon KELLY, Andrew LEECH, Caroline MAS, Daumantas MATULIS, Stephen H MCLAUGHLIN, Roland MONTSERRET, Rouba NASREDDINE, Reine NEHME, Quyen NGUYEN, David ORTEGA-ALARCON, Kathryn PEREZ, Katja PIRC, Grzegorz PISZCZEK, Marjetka PODOBNIK, Natalia RODRIGO, Jasmina ROKOV-PLAVEC, Susanne SCHAEFER, Tim SHARPE, June SOUTHALL, David STAUNTON, Pedro TAVARES, Ondrej VANEK, Michael WEYAND and Di WU.
Edition European Biophysics Journal With Biophysics Letters, NEW YORK, SPRINGER, 2021, 0175-7571.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10610 Biophysics
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 2.095
RIV identification code RIV/00216224:14740/21:00124042
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1007/s00249-021-01532-6
UT WoS 000642054100001
Keywords in English MST; TRIC; Benchmark; Thermophoresis; KD; Interaction
Tags CF BIC, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 18/5/2022 13:34.
Abstract
Microscale thermophoresis (MST), and the closely related Temperature Related Intensity Change (TRIC), are synonyms for a recently developed measurement technique in the field of biophysics to quantify biomolecular interactions, using the (capillary-based) NanoTemper Monolith and (multiwell plate-based) Dianthus instruments. Although this technique has been extensively used within the scientific community due to its low sample consumption, ease of use, and ubiquitous applicability, MST/TRIC has not enjoyed the unambiguous acceptance from biophysicists afforded to other biophysical techniques like isothermal titration calorimetry (ITC) or surface plasmon resonance (SPR). This might be attributed to several facts, e.g., that various (not fully understood) effects are contributing to the signal, that the technique is licensed to only a single instrument developer, NanoTemper Technology, and that its reliability and reproducibility have never been tested independently and systematically. Thus, a working group of ARBRE-MOBIEU has set up a benchmark study on MST/TRIC to assess this technique as a method to characterize biomolecular interactions. Here we present the results of this study involving 32 scientific groups within Europe and two groups from the US, carrying out experiments on 40 Monolith instruments, employing a standard operation procedure and centrally prepared samples. A protein–small molecule interaction, a newly developed protein–protein interaction system and a pure dye were used as test systems. We characterized the instrument properties and evaluated instrument performance, reproducibility, the effect of different analysis tools, the influence of the experimenter during data analysis, and thus the overall reliability of this method.
Links
LM2018127, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
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