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Quaternary Structure Analyses of an Essential Oligomeric Enzyme.
- Source :
-
Methods in enzymology [Methods Enzymol] 2015; Vol. 562, pp. 205-23. Date of Electronic Publication: 2015 Aug 13. - Publication Year :
- 2015
-
Abstract
- Here, we review recent studies aimed at defining the importance of quaternary structure to a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate the complementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugation with enzyme kinetics, in vitro mutagenesis, macromolecular crystallography, small angle X-ray scattering, and molecular dynamics simulations, to demonstrate the role of subunit self-association in facilitating protein dynamics and enzyme function. This multitechnique approach has yielded new insights into the molecular evolution of protein quaternary structure.<br /> (© 2015 Elsevier Inc. All rights reserved.)
- Subjects :
- Bacterial Proteins isolation & purification
Evolution, Molecular
Hydro-Lyases isolation & purification
Kinetics
Molecular Dynamics Simulation
Plant Proteins isolation & purification
Protein Multimerization
Protein Structure, Quaternary
Protein Subunits
Scattering, Small Angle
Ultracentrifugation
X-Ray Diffraction
Bacterial Proteins chemistry
Hydro-Lyases chemistry
Plant Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1557-7988
- Volume :
- 562
- Database :
- MEDLINE
- Journal :
- Methods in enzymology
- Publication Type :
- Academic Journal
- Accession number :
- 26412653
- Full Text :
- https://doi.org/10.1016/bs.mie.2015.06.020