The team also showed that they could block one link in the polymer "windmill" to create linear chains of GFP units, up to 15 units in length. 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).
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