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Assessing and Improving Protein Sample Quality

Title data

Raynal, Betrand ; Brûlé, Sébastien ; Uebel, Stephan ; Knauer, Stefan H.:
Assessing and Improving Protein Sample Quality.
In: Daviter, Tina ; Johnson, Christopher M. ; McLaughlin, Stephen H. ; Williams, Mark A. (ed.): Protein-Ligand Interactions : Methods and Applications. - New York : Springer , 2021 . - pp. 3-46 . - (Methods in Molecular Biology ; 2263 )
ISBN 978-1-0716-1197-5
DOI: https://doi.org/10.1007/978-1-0716-1197-5_1

Abstract in another language

One essential prerequisite of any experiment involving a purified protein, such as interaction studies or structural and biophysical characterization, is to work with a “good-quality” sample in order to ensure reproducibility and reliability of the data. Here, we define a “good-quality” sample as a protein preparation that fulfills three criteria: (1) the preparation contains a protein that is pure and soluble and exhibits structural and functional integrity, (2) the protein must be structurally homogeneous, and (3) the preparation must be reproducible. To ensure effective quality control (QC) of all these parameters, we suggest to follow a simple workflow involving the use of gel electrophoresis, light scattering, and spectroscopic experiments. We describe the techniques used in every step of this workflow and provide easy-to-use standard protocols for each step.

Further data

Item Type: Article in a book
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Chair Biopolymers - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 21 May 2021 05:26
Last Modified: 21 May 2021 05:26
URI: https://eref.uni-bayreuth.de/id/eprint/65268