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Biology of Shapeshifting Proteins

            There has been an almost exponential growth of innovation in the field of Biology over the years and one recently talked about are designer or shape shifting proteins. Proteins play a fundamental role both in complex and simple organisms. As we know proteins are vital to the organism in terms of functionality and purpose. With the implementation of newly designed proteins these functions can be both altered and carried out in different unique ways. In order to be able to modify proteins do to specific jobs the first thing one must do is understand the way proteins behave. Scientists have been researching and recording how different proteins behave and respond in certain conditions. Proteins have the ability to become soluble or insoluble based on changes in the environment's temperature or by other environmental conditions. In understanding the way a protein responds in certain environments and conditions they can produce the results as a set of rules to abide by. Once scientists deciphered these set of rules they realized they could manipulate these proteins in have them perform unique functions on demand.
             Amino acids form the basic structure of the proteins and in knowing these specific amino acid sequences can be exploited in order to create proteins with unique characteristics and functionality. The amino acids folding up into 3D structures are what give each protein its unique function and qualities. There are numerous different variants of amino acid sequences that can be made but there needed to be a starting point in which scientists could building a library of specific variations of certain sequences. The first protein that went into testing was elastin-like proteins. When testing their synthetic designs of elastin-like proteins they based the sequences off of five key amino acids. Using engineered E. Coli; the team grew proteins with this sequence to test their designs. After isolating the proteins scientists watched to se if the proteins would shift from soluble to insoluble forms when prompted.

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