Characterization of conformational and oligomeric states of proteins
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...
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| Format: | Book Chapter |
| Language: | English English |
| Published: |
Springer Nature Singapore
2018
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| Online Access: | http://irep.iium.edu.my/70505/ http://irep.iium.edu.my/70505/ http://irep.iium.edu.my/70505/1/70505_Characterization%20of%20conformational.pdf http://irep.iium.edu.my/70505/7/70505_Characterization%20of%20conformational_Scopus.pdf |
| Summary: | 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. |
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