Development of 48-condition buffer screen for protein stability
assessment

a 2021

Development of 48-condition buffer screen for protein stability assessment

HOUSER, Josef, Jana KOSOUROVÁ, Monika KUBÍČKOVÁ a Michaela WIMMEROVÁ

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

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

Změněno: 4. 2. 2024 14:47, Mgr. Josef Houser, Ph.D.

Anotace

V originále

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 VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

Citovat

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.

@proceedings{2252464,
   author = {Houser, Josef and Kosourová, Jana and Kubíčková, Monika and Wimmerová, Michaela},
   booktitle = {XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section},
   keywords = {protein stability; buffer scren; biophysical characterization},
   language = {eng},
   isbn = {978-80-907779-1-0},
   title = {Development of 48-condition buffer screen for protein stability assessment},
   year = {2021}
}

TY  - CONF
ID  - 2252464
AU  - Houser, Josef - Kosourová, Jana - Kubíčková, Monika - Wimmerová, Michaela
PY  - 2021
TI  - Development of 48-condition buffer screen for protein stability assessment
SN  - 9788090777910
KW  - protein stability
KW  - buffer scren
KW  - biophysical characterization
N2  - 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.
ER  -

HOUSER, Josef, Jana KOSOUROVÁ, Monika KUBÍČKOVÁ a Michaela WIMMEROVÁ. Development of 48-condition buffer screen for protein stability assessment. In \textit{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.

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