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 a 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, roč. 50, 3-4, s. 411-427. ISSN 0175-7571. Dostupné z: https://dx.doi.org/10.1007/s00249-021-01532-6.
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Základní údaje
Originální název Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study
Autoři 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 Česká republika, domácí), Josef HOUSER (203 Česká republika, domácí), 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 a Di WU.
Vydání European Biophysics Journal With Biophysics Letters, NEW YORK, SPRINGER, 2021, 0175-7571.
Další údaje
Originální jazyk angličtina
Typ výsledku Článek v odborném periodiku
Obor 10610 Biophysics
Stát vydavatele Spojené státy
Utajení není předmětem státního či obchodního tajemství
WWW URL
Impakt faktor Impact factor: 2.095
Kód RIV RIV/00216224:14740/21:00124042
Organizační jednotka Středoevropský technologický institut
Doi http://dx.doi.org/10.1007/s00249-021-01532-6
UT WoS 000642054100001
Klíčová slova anglicky MST; TRIC; Benchmark; Thermophoresis; KD; Interaction
Štítky CF BIC, rivok
Příznaky Mezinárodní význam, Recenzováno
Změnil Změnila: Mgr. Pavla Foltynová, Ph.D., učo 106624. Změněno: 18. 5. 2022 13:34.
Anotace
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.
Návaznosti
LM2018127, projekt VaVNázev: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology
VytisknoutZobrazeno: 18. 7. 2024 20:18