Ramius Posted July 12, 2006 Share Posted July 12, 2006 If what you posted made any sense whatsoever, it still wouldn't have anything to do with the topic. There's no violation of thermodynamics in the process, any more than there is writing data to magnetic media. You didn't "thwart" me. You just once again are throwing big words out that you don't understand, and hoping against hope that just one of them sticks. 721997[/snapback] i question how long the protein itself can functionally last on the surface of these DVD's. Hes shown that it can stay in the excited state for long periods of time, but eventually the protein will degrade and breakdown. I'd hate to lose gigs of data because i licked my finger and rubbed the DVD to get a spot off of it. interesting technology tho, and i will be interested to see how this progresses. Link to comment Share on other sites More sharing options...
Crap Throwing Monkey Posted July 12, 2006 Share Posted July 12, 2006 What a profund case of ego over sense. When you can go - as well as that professaor - and strain a molecule via bending without imparting and maintaing the application of energy, book your tickets for your Oslo prize. ..for you've changed understanding. Now, don't have a fit... 722003[/snapback] It's an inherent property of the molecule you dolt. Read 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 colour before returning to its 'ground state'. Since the intermediates generally only last for hours or days, Prof Renugopalakrishnan and his colleagues modified the DNA that produces bR protein to produce an intermediate that lasts for more than several years. That's not a violation of conservation of energy. That's STORAGE of energy. Jesus H. !@#$ing Christ on a pony. I can't believe I share a planet with morons like you. Link to comment Share on other sites More sharing options...
Crap Throwing Monkey Posted July 12, 2006 Share Posted July 12, 2006 i question how long the protein itself can functionally last on the surface of these DVD's. Hes shown that it can stay in the excited state for long periods of time, but eventually the protein will degrade and breakdown. I'd hate to lose gigs of data because i licked my finger and rubbed the DVD to get a spot off of it. interesting technology tho, and i will be interested to see how this progresses. 722004[/snapback] I thought the same thing. Seems better suited to a flash memory application. All storage degrades eventually, even DVDs...but "a few years" just wouldn't cut it for any storage device with any sort of pretension to permanence. I question how you can usefully bind them to a media, too. It's entirely possible for the binding to affect the storage properties of the molecule adversely. But like I said: principle is easy. Engineering's a B word. Link to comment Share on other sites More sharing options...
stuckincincy Posted July 12, 2006 Share Posted July 12, 2006 It's an inherent property of the molecule you dolt. Read the article. That's not a violation of conservation of energy. That's STORAGE of energy. Jesus H. !@#$ing Christ on a pony. I can't believe I share a planet with morons like you. 722006[/snapback] Oh come on. The charlatan's "Yahoo" article ended with his words "Science can be used and abused. Making large amounts of information so portable on high-capacity removable storage devices will make it easier for information to fall into the wrong hands. Information can be stolen very quickly. One has to have some safeguards there," he added." Did a bell or whistle go off? Perhaps the slightest doubt of his claims? Perhaps that his touted molecules aren't STORAGE devices? Perhaps legit entities have explored similar avenues yet are silent? Link to comment Share on other sites More sharing options...
MattyT Posted July 12, 2006 Share Posted July 12, 2006 I question how you can usefully bind them to a media, too. It's entirely possible for the binding to affect the storage properties of the molecule adversely. But like I said: principle is easy. Engineering's a B word. 722011[/snapback] That's what I'm really curious about...how to get the molecules from doing a performance suited for the Rockettes to saving all my porn. Some kind of optical drive maybe? But then I wonder about what a laser would do to a molecule. Cool stuff. Link to comment Share on other sites More sharing options...
Crap Throwing Monkey Posted July 12, 2006 Share Posted July 12, 2006 Did a bell or whistle go off? Perhaps the slightest doubt of his claims? Perhaps that his touted molecules aren't STORAGE devices? Perhaps legit entities have explored similar avenues yet are silent? 722021[/snapback] What??? Now you think he's building bombs now or something? If I ever need a brain transplant, can I have yours? I want one that's never been used... Link to comment Share on other sites More sharing options...
Crap Throwing Monkey Posted July 12, 2006 Share Posted July 12, 2006 That's what I'm really curious about...how to get the molecules from doing a performance suited for the Rockettes to saving all my porn. Some kind of optical drive maybe? But then I wonder about what a laser would do to a molecule. Cool stuff. 722027[/snapback] That's in the article: a laser (light) pops the molecule into an excited state (an excited metastable state, cincy). The big engineering issue I see right off the top of my head is: molecules are attached to substrate with a binding energy of X, molecules get kicked into an excited "on" state with an incident energy of Y, laser has an energy of Z (actually, Z per unit area or volume per unit time...but anyway...). If X is greater than Y by too much, can the molecules be excited? If Y is greater than X, do the molecules stay attached to the substrate when excited? If Z is greater than Y (as it has to be), is it still less than X or will it rip the molecules off the substrate? But that's "just" engineering. The principle is sound, at least. Link to comment Share on other sites More sharing options...
Dan Gross Posted July 12, 2006 Share Posted July 12, 2006 That's what I'm really curious about...how to get the molecules from doing a performance suited for the Rockettes to saving all my porn. Some kind of optical drive maybe? But then I wonder about what a laser would do to a molecule. Cool stuff. 722027[/snapback] Well, see, the lasers project molecule porn, which gets the molecules excited.... If we can figure out how to get those crazy othogonally polarized glasses made small enough for the molecules to wear, we could probably jam even more storage on there... Link to comment Share on other sites More sharing options...
Crap Throwing Monkey Posted July 12, 2006 Share Posted July 12, 2006 If we can figure out how to get those crazy othogonally polarized glasses made small enough for the molecules to wear, we could probably jam even more storage on there... 722051[/snapback] Ball bearings! Awww, come on, it's so simple. It's all ball bearings nowadays. Link to comment Share on other sites More sharing options...
Guffalo Posted July 12, 2006 Share Posted July 12, 2006 A certain molecule, when exposed to light, bends itself into a certain shape. When the light's removed, it returns to its original shape. Was it really that complex? I'm seriously asking...I thought it was self-evident. 721891[/snapback] Sound like me on the morning of a severe overhang. Link to comment Share on other sites More sharing options...
MattyT Posted July 12, 2006 Share Posted July 12, 2006 Ball bearings! Awww, come on, it's so simple. It's all ball bearings nowadays. 722056[/snapback] Yeah. 220, 221....whatever it takes. Link to comment Share on other sites More sharing options...
Johnny Coli Posted July 12, 2006 Share Posted July 12, 2006 I question how you can usefully bind them to a media, too. It's entirely possible for the binding to affect the storage properties of the molecule adversely. 722011[/snapback] It's a membrane-bound protein, so you could conceivably pack them in pretty tight into some hydrophobic matrix. I would imagine they'd be pretty stable in a system like that, as proteins are quite happy under those conditions. The only problem I could see would be how much conformational change the protein needs to go through in order to get the desired effect. It is my understanding though, that the actual excitation/relaxation is done by the retinal molecule attached to the bacteriorhodopsin. It's the retinal that is light-sensitive, and it's the protein that facilitates pushing the protons across the cell membrane. If you're just looking for a color change, and not for proton translocation, you wouldn't need the protein to move that much, if at all. The retinal/chromophore color change is really all you'd be interested in. So you'd just need them packed in pretty tight in some crystalline/lattice monolayer. At least that was my understanding of the article. They've actually been working with these types of phototransducing molecules for a while in bioengineering and nanotech research. Bacteriorhodopsin was the first membrane protein they got a structure for, way back in the early 70's. They've done a fair amount of work using them in getting current through membranes, as they are proton pumps, after all. Link to comment Share on other sites More sharing options...
MattyT Posted July 12, 2006 Share Posted July 12, 2006 It's a membrane-bound protein, so you could conceivably pack them in pretty tight into some hydrophobic matrix. I would imagine they'd be pretty stable in a system like that, as proteins are quite happy under those conditions. The only problem I could see would be how much conformational change the protein needs to go through in order to get the desired effect. It is my understanding though, that the actual excitation/relaxation is done by the retinal molecule attached to the bacteriorhodopsin. It's the retinal that is light-sensitive, and it's the protein that facilitates pushing the protons across the cell membrane. If you're just looking for a color change, and not for proton translocation, you wouldn't need the protein to move that much, if at all. The retinal/chromophore color change is really all you'd be interested in. So you'd just need them packed in pretty tight in some crystalline/lattice monolayer. At least that was my understanding of the article. They've actually been working with these types of phototransducing molecules for a while in bioengineering and nanotech research. Bacteriorhodopsin was the first membrane protein they got a structure for, way back in the early 70's. They've done a fair amount of work using them in getting current through membranes, as they are proton pumps, after all. 722062[/snapback] I fold. Link to comment Share on other sites More sharing options...
stuckincincy Posted July 12, 2006 Share Posted July 12, 2006 What??? Now you think he's building bombs now or something? If I ever need a brain transplant, can I have yours? I want one that's never been used... 722040[/snapback] Bombs? Be bendable like molecules, I a I lead to belive...that's the ticket. Did a little search about your guru VR here. Stop it, CTM. We have a techinical dispute and you diminish yourself with your use of insults. Link to comment Share on other sites More sharing options...
Crap Throwing Monkey Posted July 12, 2006 Share Posted July 12, 2006 It's a membrane-bound protein, so you could conceivably pack them in pretty tight into some hydrophobic matrix. I would imagine they'd be pretty stable in a system like that, as proteins are quite happy under those conditions. The only problem I could see would be how much conformational change the protein needs to go through in order to get the desired effect. It is my understanding though, that the actual excitation/relaxation is done by the retinal molecule attached to the bacteriorhodopsin. It's the retinal that is light-sensitive, and it's the protein that facilitates pushing the protons across the cell membrane. If you're just looking for a color change, and not for proton translocation, you wouldn't need the protein to move that much, if at all. The retinal/chromophore color change is really all you'd be interested in. So you'd just need them packed in pretty tight in some crystalline/lattice monolayer. At least that was my understanding of the article. They've actually been working with these types of phototransducing molecules for a while in bioengineering and nanotech research. Bacteriorhodopsin was the first membrane protein they got a structure for, way back in the early 70's. They've done a fair amount of work using them in getting current through membranes, as they are proton pumps, after all. 722062[/snapback] But...but...but...that violates the Second Law of Thermodynamics!!! Link to comment Share on other sites More sharing options...
Crap Throwing Monkey Posted July 12, 2006 Share Posted July 12, 2006 Stop it, CTM. We have a techinical dispute and you diminish yourself with your use of insults. 722065[/snapback] Actually, our original dispute is over the Second Law of Thermodynamics and your near-utter lack of reading comprehension. Which, frankly, makes you damned lucky I diminish myself by responding to your idiocy. Link to comment Share on other sites More sharing options...
inkman Posted July 12, 2006 Share Posted July 12, 2006 It's a membrane-bound protein, so you could conceivably pack them in pretty tight into some hydrophobic matrix. I would imagine they'd be pretty stable in a system like that, as proteins are quite happy under those conditions. The only problem I could see would be how much conformational change the protein needs to go through in order to get the desired effect. It is my understanding though, that the actual excitation/relaxation is done by the retinal molecule attached to the bacteriorhodopsin. It's the retinal that is light-sensitive, and it's the protein that facilitates pushing the protons across the cell membrane. If you're just looking for a color change, and not for proton translocation, you wouldn't need the protein to move that much, if at all. The retinal/chromophore color change is really all you'd be interested in. So you'd just need them packed in pretty tight in some crystalline/lattice monolayer. At least that was my understanding of the article. They've actually been working with these types of phototransducing molecules for a while in bioengineering and nanotech research. Bacteriorhodopsin was the first membrane protein they got a structure for, way back in the early 70's. They've done a fair amount of work using them in getting current through membranes, as they are proton pumps, after all. 722062[/snapback] Uh... Hmmmm... Where's the peepee joke threads? Link to comment Share on other sites More sharing options...
Johnny Coli Posted July 12, 2006 Share Posted July 12, 2006 I fold. 722063[/snapback] Sorry man. I'm a microbiologist, and have a real soft spot for Arhcaea, which is really what Halobacterium are. Woese is me every time I hear them referred to as "bacteria." That being said, this a just a form of photosynthesis, like plants do, but without the chlorophyll. They're remarkable little dynamos, and survive in some incredibally harsh environments. There's absolutely nothing they can't do, or can't be trained to do. Link to comment Share on other sites More sharing options...
MattyT Posted July 12, 2006 Share Posted July 12, 2006 Sorry man. I'm a microbiologist, and have a real soft spot for Arhcaea, which is really what Halobacterium are. Woese is me every time I hear them referred to as "bacteria." That being said, this a just a form of photosynthesis, like plants do, but without the chlorophyll. They're remarkable little dynamos, and survive in some incredibally harsh environments. There's absolutely nothing they can't do, or can't be trained to do. 722074[/snapback] Franks and beans! Franks and beans! Link to comment Share on other sites More sharing options...
IDBillzFan Posted July 12, 2006 Share Posted July 12, 2006 I fold. 722063[/snapback] That was damn funny. Link to comment Share on other sites More sharing options...
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