Protein Memory

Protein Adds Muscle to Computer Memory
In recent news that seems more science fiction than applied science, Japanese researchers have unveiled exciting new research that could change the way we create and use computers in years to come. Japanese professor Tetsuro Majima of Osaka University has demonstrated that proteins -- once the concern of chemists and biologists -- could now have impressive potential in the world of computer science. (Source: livescience.com)
Majima's research has indicated that proteins isolated from select bacteria species are able to store computer data, and that this type of storage could exceed the capabilities of current magnetic and optical storage components.
The fluorescent bacterial protein is etched onto glass, and read using precise combinations of light and chemicals. The data can be read, manipulated, and erased in a manner almost identical to current computer memory devices.
Typical computer memory circuits are manufactured using metal arranged on silicon. Since the manufacturing process requires extremely high temperatures it is usually impossible for thin materials like plastic or glass to be used as circuits since they cannot withstand the necessary high temperatures. (Source: pinktentacle.com)
Protein-based memory devices will not require the use of high-temperature manufacturing, and will therefore be able to incorporate much thinner materials than traditional optical and magnetic-based memory systems.
The proteins can be "fixed" (etched with information) in about one minute, a speed that will improve as the technology is further developed. Along with fairly rapid information recording, memory devices based on protein will likely be unaffected by magnetic interference and will remain relatively stable at temperatures lower than the typical computer.
Protein-based memory promises users a faster, more efficient and more reliable form of data relay than current technologies, and one that will likely come in a much smaller package. The use of thinner materials will allow developers to create much smaller devices that will greatly expand the range of applications possible for protein technology.
With so many desirable qualities, it's no surprise that Majima's team is not the first to think of using proteins as a computer storage device. Researchers have been exploring the applications of various proteins for use in computer memory since 1995. (Source: msu.edu)
Last year, another Japanese research team at the Naro Institute of Science and Technology (NAIST) developed a protein-based computer memory component based on the protein ferritin, an iron-storing protein common to mammals and also to certain forms of bacteria. NAIST has not yet published definitive results although they expect to be at the product development stage within the next few years.
The applications of protein-based storage are intended primarily for a commercial market, but Majima also hopes to develop applications that will ameliorate the function of various medical devices and test procedures. Majima hopes to have a commercially viable product developed within the next five years.
A thinner, faster computer is definitely appealing to most consumers, and protein-based memory devices do seem to hold a lot of potential in that area. As the fields of biology and computer science converge, it will be interesting to discover what other biological molecules have potential computing applications. Perhaps we will succeed in creating an intelligent machine that is a fusion of living and artificial components. If current research efforts are any indication of the future of computer development, "Resistance is futile."

Researchers tout progress towards protein-based memory device

There's certainly no shortage of research going on into unconventional means of storage, but one of the most unusual has to be protein-based storage, which we haven't heard much of in quite a while. That now looks to have changed, however, with some researchers in Japan boasting that they've made some considerable progress with the so-called "recordable proteins." To that end, Tetsuro Majima and his team reportedly employed a special fluorescent protein to record an information pattern on a glass slide, along with what's described only as a "novel combination of light and chemicals" to read and, most importantly, erase that information. While it's obviously a long ways from replacing your hard drive, the researchers apparently see no shortage of potential applications for the technology, including using the proteins to improve biosensors and diagnostic tests.

Protein memory through altered folding mediated by intramolecular chaperones
U. P. Shinde1, J. J. Liu1 & M. Inouye1
1. Department of Biochemistry, Robert Wood Johnson Medical School-UMDNJ, 675 Hoes Lane, Piscataway, New Jersey 08854, USA
Correspondence to: M. Inouye1 Correspondence and requests for materials should be addressed to M.I. (e-mail: Email: inouye@rwja.umdnj.edu).
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The 77-residue propeptide of subtilisin acts as an intramolecular chaperone that organizes the correct folding of its own protease domain. Similar folding mechanisms are used by several prokaryotic and eukaryotic proteins, including prohormone-convertases. Here we show that the intramolecular chaperone of subtilisin facilitates folding by acting as a template for its protease domain, although it does not form part of that domain. Subtilisin E folded by an intramolecular chaperone with an Ile(-48)-to-Val mutation acquires an 'altered' enzymatically active conformation that differs from wild-type subtilisin E. Although both the altered and wild-type subtilisins have identical amino-acid sequences, as determined by amino-terminal sequencing and mass spectrometry, they bind their cognate intramolecular chaperones with 4.5-fold greater affinity than non-cognate intramolecular chaperones, when added in trans. The two subtilisins also have different secondary structures, thermostability and substrate specificities. Our results indicate that an identical polypeptide can fold into an altered conformation through a mutated intramolecular chaperone and maintains memory of the folding process. Such a phenomenon, which we term 'protein memory', may be important in investigations of protein folding.