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Bacterial DVD Holds 50TB

CAMags writes to tell us that a Harvard Professor is claiming to have developed a new variant of a protein called bacteriorhodopsin (bR) that, when layered on a DVD, can store up to 50TB of data. From the article: "The light-activated protein is found in the membrane of a salt marsh microbe Halobacterium salinarum and is also known as bacteriorhodopsin (bR). It captures and stores sunlight to convert it to chemical energy. When light shines on bR, it is converted to a series of intermediate molecules each with a unique shape and color before returning to its 'ground state.'"

8 of 268 comments (clear)

  1. A whole new era for Sneaker-Net by IndustrialComplex · · Score: 5, Interesting

    Imagine the datarate if I were to hop into my car, drive across the country, and load this disk into a computer in California.

    Even if the trip takes me 48 hours, that is still 303 MB/s!

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    Out of modpoints but really liked a post? 1BDkF6TtmmeZ3yqXbz9yhdYVqRYnwFoXDj
  2. rhodopsin difficulties by Anonymous Coward · · Score: 1, Interesting

    I think it's worth mentioning that the protein in question is notoriously difficult to work with. As a G-protein-coupled-receptor (GPCR), it's normally found spanning a cell membrane: aka imbedded in lipids (fats). This makes it very difficult to work with from a solubility/structure standpoint.

    Depending on what you consider acceptable for a structure, people have only known the atomic-level details of rhodopsin for the last few years (http://tinyurl.com/jtj6gPDB). Bacteriorhodopsin has been a bit more accessible, but it too is a fairly recent structure. For a protein as highly studied as this family is, that's not much time at all. This is why so much effort has been placed on really convoluted methods to obtain the structural information indirectly. For one example that involved some computational methods, see http://tinyurl.com/kawwr.

    And here's another thought for you: GPCRs transmit a photon signal to a physically-transmitted biochemical cascade. So although you can make rhodopsin change conformation with the right light-based input, how can you read the structurally-conferred output?

    Although I appreciate the fundamental science being carried out by the research group mentioned, I think it's bad form to mislead the general public with overreaching claims. If you're really interested in high-capacity storage, I think that the engineered protein cages, based upon viral capsids and similar structures, have more potential for nano-level storage as a means to create highly regular, tailored metallic materials.

  3. Re:Quit repeating the stupid myth by WillyPete · · Score: 2, Interesting

    That's true as far as it goes, which is right out the window.

    If we can agree that fuel efficient cars were are a good idea now, they would have been an even better idea in the 70's (or earlier). It might have even made a significant impact by now.

    We didn't, and it wasn't because we couldn't.

    The real myth is that textbooks provide hard rules that actually translate universally into the real word. If people were satisfied with following the rules, we'd all be communists.

    --
    Shaw's Principle: Build a system even a fool could use, and only a fool would want to use it.
  4. An embarassment to chemists everywhere by liegeofmelkor · · Score: 2, Interesting

    His claim of terabyte storage shows an extreme naivety (or one could argue ignorance) of fundamental physical principles the good doctor should be aware of. It is true that there must be some medium capable of handling data storage on such a small scale, but the real hang-up, at least in terms of commercial viability, is the light source which reads the medium. Any dolt who knows next to nothing about high definition dvd's at least knows the major technological innovation involved is a commercially available blue light source (blue puts the Blu in Blu-Ray), not any groundbreaking technology involving the discs (though to save myself from flamebait, there have been advances here). Now, traditional dvd's/cd's are in the 700nm range, high def systems are around 400nm, and the industrial systems used to make microchips (yeah, these are expensive and not at all portable) can only burn chips 45nm thick. A light source of a couple nanometers (the quantity he uses for his predicted size) puts us into the soft x-ray range. Big deal if we have a storage medium. We won't be able to read or write to it (cheaply enough for consumers, that is) for decades. If I were this guy's employer, I'd investigate whether he ever completed a bachelor's degree in science, much less a PhD. This is a fundamental oversight on his part.

    1. Re:An embarassment to chemists everywhere by liegeofmelkor · · Score: 2, Interesting

      Doh, making myself look as big an idiot as Dr V. The property of bacteriorhodopsin he's manipulating involves absorption/reflection in the visible spectrum, meaning you must use a visible light source to read/write... meaning you won't ever be able to use rhodopsin to read at the ~1nm length scale, because you can't focus a 400nm wavelength spot to 1nm. A focused, soft x-ray source does you no good. What an idiot (him and me both).

  5. OT: Small World... by evilviper · · Score: 2, Interesting
    From TFA:
    Sydney, Jul 8 (ANI): An Indian born scientist in the US is working on

    Does anyone else find it ironic that /. (which is a US-based site--with readers from around the world) posts a link to an article from an Australia news site, talking about developments of an Indian-born scientist, working in the US?
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    Slashdot gets worse every day... Pipedot: News for nerds, without the corporate slant
  6. Re:I bet these will have the same problem as CD-RW by fafalone · · Score: 4, Interesting

    So what if it degrades? I'd still love to have 50TB discs that last for 2-3 years instead of a few GB that lasts a few years. This is a new technology designed to give higher capacity, not longer shelf life.

  7. Re:I read this in a science book by detritus` · · Score: 2, Interesting

    They're doing amazing work with protein folding, but even if you can semi predict how the protein is going to fold, it doesnt help as we cant currently say this is the configuration we want, with these amino acids at these sites, how would we make it? It getting there but there's still a lot of work to do