HOUSER, Josef, Jana KOSOUROVÁ, Monika KUBÍČKOVÁ a Michaela WIMMEROVÁ. Development of 48-condition buffer screen for protein stability assessment. In XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section. 2021. ISBN 978-80-907779-1-0.
Další formáty:   BibTeX LaTeX RIS
Základní údaje
Originální název Development of 48-condition buffer screen for protein stability assessment
Autoři HOUSER, Josef (203 Česká republika, garant, domácí), Jana KOSOUROVÁ (203 Česká republika, domácí), Monika KUBÍČKOVÁ (703 Slovensko, domácí) a Michaela WIMMEROVÁ (203 Česká republika, domácí).
Vydání XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section, 2021.
Další údaje
Originální jazyk angličtina
Typ výsledku Konferenční abstrakt
Obor 10610 Biophysics
Stát vydavatele Česká republika
Utajení není předmětem státního či obchodního tajemství
Kód RIV RIV/00216224:14740/21:00130284
Organizační jednotka Středoevropský technologický institut
ISBN 978-80-907779-1-0
Klíčová slova česky stabilita proteinu; buffer screen; biofyzikální charakterizace
Klíčová slova anglicky protein stability; buffer scren; biophysical characterization
Změnil Změnil: Mgr. Josef Houser, Ph.D., učo 77781. Změněno: 4. 2. 2024 14:47.
Anotace
The determination of a suitable buffer environment for a protein of interest is not an easy task. The choice of the buffer is important both for basic research and for scaling up for use in biotechnologies. However, the requirements of advanced techniques, the demands on the biological material, and the researcher time needed for buffer optimization, as well as personal inflexibility, lead frequently to the use of sub-optimal buffers. Here, we demonstrate the design of a 48-condition buffer screen that can be used to determine an appropriate environment for downstream studies [1]. By the combination of several techniques (differential scanning fluorimetry, dynamic light scattering, and bio-layer interferometry), we are able to assess the protein stability, homogeneity, and binding activity across the screen with as little as 100 μg of protein in 1 day. The application of this screen helps to avoid unsuitable conditions, explain problems observed upon protein analysis, and choose the most suitable buffers for further research and applications. The screen can be routinely used as a primary screen for buffer optimization in laboratories and facilities.
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: 23. 7. 2024 17:34