#Scaffold protein assembly free#
Proteins were then genetically linked to the free ends of each GFP monomer “blade”. The team was able to separate the polymers based on their sizes. A four-bladed polymer, for example, is composed of four monomers linked together to form a tetramer. The researchers discovered that each polymer was organized in a polygonal shape resembling a windmill with 2 to 10 blades, each blade representing a GFP monomer. This monomer then self-assembles with other GFP monomers to form polymers. A GFP monomer was designed to have these two linking units. The team formed the scaffold by taking advantage of the fact that two different GFP units with specific chains of GFP amino acids can be spontaneously linked in a bacterial cell. Because of its fluorescent properties, making it easy to see, it has been widely used in research. It is commonly found in some fluorescing marine animals such as jellyfish. GFP is a fluorescent protein composed of 238 amino acid residues. The KAIST team has developed a set of green fluorescent protein (GFP) assemblies with relatively simple, well-defined structures that can be powerful scaffolds for assembling other proteins. Their findings form a big step in discovering better ways to build diverse protein assemblies with new structures and functions. That may be about to change, say scientists at the Korea Advanced Institute of Science and Technology (KAIST). But the sheer complexity of protein structures makes it extremely challenging to understand and assemble them at a basic level. doi: 10.1016/j.cej.2017.11.030.Large protein assemblies have a wealth of potential uses, such as in drug and vaccine development or in the production of chemicals, fuels or agricultural additives. Immobilization of cellulase on styrene/maleic anhydride copolymer nanoparticles with improved stability against pH changes. Wang Y., Chen D., Wang G., Zhao C., Ma Y., Yang W. Facile fabrication of electrochemical ZnO nanowire glucose biosensor using roll to roll printing technique. Immobilization of lipase onto novel constructed polydopamine grafted multiwalled carbon nanotube impregnated with magnetic cobalt and its application in synthesis of fruit flavours. Nanobiocatalysis and its potential applications. Identification of a multi-enzyme complex for glucose metabolism in living cells. Kohnhorst C.L., Kyoung M., Jeon M., Schmitt D.L., Kennedy E.L., Ramirez J.…An S. Such mega-enzyme complexes promise wider applications in the field of biotechnology and bioengineering.īinding modules Dockerin-cohesin interactions Multi-enzyme complex Protein scaffolds SpyTag-Sp圜atcher system. Various analytical and characterization tools that have enabled the development of these scaffolding strategies are also reviewed. Moreover, different conjugation strategies viz dockerin-cohesin interaction, SpyTag-Sp圜atcher system, peptide linker-based ligation, affibody, and sortase-mediated ligation are discussed in detail. This review describes the components of protein scaffolds, different ways of constructing a protein scaffold-based multi-enzyme complex, and their effects on enzyme kinetics. The scaffolding improves the catalytic performance, enzyme stability and provides an optimal micro-environment for biochemical reactions. With this respect, scaffolding proteins play an immense role in bringing different enzymes together in a specific manner. However, operating different enzymes together in a single vessel limits their operational performance which needs to be addressed. The synthesis of complex molecules using multiple enzymes simultaneously in one reaction vessel has rapidly emerged as a new frontier in the field of bioprocess technology.
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