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 and Michaela WIMMEROVÁ

Basic information

Original name

Development of 48-condition buffer screen for protein stability assessment

Authors

HOUSER, Josef (203 Czech Republic, guarantor, belonging to the institution), Jana KOSOUROVÁ (203 Czech Republic, belonging to the institution), Monika KUBÍČKOVÁ (703 Slovakia, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, belonging to the institution)

Edition

XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section, 2021

Other information

Language

English

Type of outcome

Konferenční abstrakt

Field of Study

10610 Biophysics

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

RIV identification code

RIV/00216224:14740/21:00130284

Organization unit

Central European Institute of Technology

ISBN

978-80-907779-1-0

Keywords (in Czech)

stabilita proteinu; buffer screen; biofyzikální charakterizace

Keywords in English

protein stability; buffer scren; biophysical characterization

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

Abstract

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.

Links

LM2018127, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

HOUSER, Josef, Jana KOSOUROVÁ, Monika KUBÍČKOVÁ and 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 and 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.

Detailed Information on Publication Record