Development of 48-condition buffer screen for protein stability
assessment

J 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 (203 Česká republika, domácí) a Michaela WIMMEROVÁ (203 Česká republika, domácí)

Vydání

European Biophysics Journal With Biophysics Letters, NEW YORK, SPRINGER, 2021, 0175-7571

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.095

Kód RIV

RIV/00216224:14740/21:00121458

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1007/s00249-021-01497-6

UT WoS

000615765400001

Klíčová slova anglicky

Protein stability; Buffer; Screening; Differential scanning fluorimetry; Dynamic light scattering; Bio-layer interferometry

Štítky

CF BIC, rivok

Změněno: 18. 5. 2022 13:08, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

The determination of a suitable buffer environment for a protein of interest is not an easy task. 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. 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 less than half a milligram of protein in 1 day. The application of this screen helps to avoid unsuitable conditions, to explain problems observed upon protein analysis and to choose the most suitable buffers for further research. The screen can be routinely used as a primary screen for buffer optimization in labs 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

LM2018131, projekt VaV

Název: Česká národní infrastruktura pro biologická data (Akronym: ELIXIR-CZ)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Česká národní infrastruktura pro biologická data

Citovat

HOUSER, Josef, Jana KOSOUROVÁ, Monika KUBÍČKOVÁ a Michaela WIMMEROVÁ. Development of 48-condition buffer screen for protein stability assessment. European Biophysics Journal With Biophysics Letters. NEW YORK: SPRINGER, 2021, roč. 50, 3-4, s. 461-471. ISSN 0175-7571. Dostupné z: https://dx.doi.org/10.1007/s00249-021-01497-6.

@article{1762616,
   author = {Houser, Josef and Kosourová, Jana and Kubíčková, Monika and Wimmerová, Michaela},
   article_location = {NEW YORK},
   article_number = {3-4},
   doi = {http://dx.doi.org/10.1007/s00249-021-01497-6},
   keywords = {Protein stability; Buffer; Screening; Differential scanning fluorimetry; Dynamic light scattering; Bio-layer interferometry},
   language = {eng},
   issn = {0175-7571},
   journal = {European Biophysics Journal With Biophysics Letters},
   title = {Development of 48-condition buffer screen for protein stability assessment},
   url = {https://link.springer.com/article/10.1007%2Fs00249-021-01497-6},
   volume = {50},
   year = {2021}
}

TY  - JOUR
ID  - 1762616
AU  - Houser, Josef - Kosourová, Jana - Kubíčková, Monika - Wimmerová, Michaela
PY  - 2021
TI  - Development of 48-condition buffer screen for protein stability assessment
JF  - European Biophysics Journal With Biophysics Letters
VL  - 50
IS  - 3-4
SP  - 461-471
EP  - 461-471
PB  - SPRINGER
SN  - 01757571
KW  - Protein stability
KW  - Buffer
KW  - Screening
KW  - Differential scanning fluorimetry
KW  - Dynamic light scattering
KW  - Bio-layer interferometry
UR  - https://link.springer.com/article/10.1007%2Fs00249-021-01497-6
N2  - The determination of a suitable buffer environment for a protein of interest is not an easy task. 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. 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 less than half a milligram of protein in 1 day. The application of this screen helps to avoid unsuitable conditions, to explain problems observed upon protein analysis and to choose the most suitable buffers for further research. The screen can be routinely used as a primary screen for buffer optimization in labs and facilities.
ER  -

HOUSER, Josef, Jana KOSOUROVÁ, Monika KUBÍČKOVÁ a Michaela WIMMEROVÁ. Development of 48-condition buffer screen for protein stability assessment. \textit{European Biophysics Journal With Biophysics Letters}. NEW YORK: SPRINGER, 2021, roč.~50, 3-4, s.~461-471. ISSN~0175-7571. Dostupné z: https://dx.doi.org/10.1007/s00249-021-01497-6.

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