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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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Abstract

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: 14 Feb 2019 12:05
URI: http://irep.iium.edu.my/id/eprint/70505

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