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Characterization of conformational and oligomeric states of proteins

Ahmad Fuad, Fazia Adyani (2018) Characterization of conformational and oligomeric states of proteins. In: Multifaceted protocol in biotechnology. Springer Nature Singapore, pp. 167-178. ISBN 978-981-13-2256-3

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Oligomerization and conformational changes of proteins in solutions are advantageous for their structural and functional control. The advancement in biophysical characterization analyses, such as Size Exclusion Chromatography coupled with Multi-Angle Light Scattering (SEC-MALS) has shed lights in understanding the underlying mechanisms of actions for protein molecules. This chapter focuses on three types of protein analysis; SEC-MALS, native PAGE and continuous enzymatic assays of the bacterially expressed cofactor-independent phosphoglycerate mutase from Leishmania mexicana (Lm-iPGAM), which was shown to exist in different oligomeric and conformational states in solution. The outcome of this analyses has paved the way towards understanding the behavior of Lm-iPGAM in solution, which is important for further structural and functional studies.

Item Type: Book Chapter
Additional Information: 7200/70505
Uncontrolled Keywords: Protein conformations and oligomeric states · Multi-Angle Light Scattering (SEC-MALS) · Native PAGE · Continuous enzymatic assays · Leishmania mexicana · Cofactor-independent phosphoglycerate mutase
Subjects: T Technology > TP Chemical technology > TP248.13 Biotechnology
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button): Kulliyyah of Engineering
Kulliyyah of Engineering > Department of Biotechnology Engineering
Depositing User: Dr Fazia Adyani Ahmad Fuad
Date Deposited: 14 Feb 2019 10:30
Last Modified: 05 Mar 2020 16:42
URI: http://irep.iium.edu.my/id/eprint/70505

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