Development of 48-condition buffer screen for protein stability assessment

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00121458" target="_blank" >RIV/00216224:14740/21:00121458 - isvavai.cz</a>

Výsledek na webu

<a href="https://link.springer.com/article/10.1007%2Fs00249-021-01497-6" target="_blank" >https://link.springer.com/article/10.1007%2Fs00249-021-01497-6</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00249-021-01497-6" target="_blank" >10.1007/s00249-021-01497-6</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Development of 48-condition buffer screen for protein stability assessment

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Development of 48-condition buffer screen for protein stability assessment

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

European Biophysics Journal With Biophysics Letters

ISSN

0175-7571

e-ISSN

—

Svazek periodika

50

Číslo periodika v rámci svazku

3-4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

461-471

Kód UT WoS článku

000615765400001

EID výsledku v databázi Scopus

2-s2.0-85100530581