Unfortunately there's no good way to define practicing versus non-practicing.
Not at all. A patent owner that really is trying to "promote the useful arts and sciences" is either trying to bring an implementation of the claimed invention to market, or is offering the patent for licensing. Virtually all patent trolls could be taken care of by requiring the plaintiff to show that they have made a good faith effort to do one of these two before they can bring a suit for infringement.
I went to the exhibit with the same question. One of the docents said that it was an engineering platform built for ground-based testing. There was an immense amount of ground-based testing and re-testing; failure of one of these satellites in orbit would have been a national security emergency.
This system already exists, and already functions better than it would if the USPTO were involved. If you want a patent to go into the public domain, do the following:
Start a nonprofit organization, like a 501(c)(3) in the USA. Legal costs for doing so are minimal compared to the purchase price of the patent.
Raise the money.
Buy the rights to the patent.
Either allow the patent to expire by not paying the maintenance fee, or by explicitly disclaiming the remaining term of the patent and granting the rights to the public domain.
Not only does this procedure not need the involvement of the USPTO, but it has the added benefit of you not needing to pay any more for the patent than the selling price the owner is willing to accept.
On the other hand, determining the "selling price" is not quite as simple as "150% of the development costs". The value of a patent is not that it is a way of recouping your development and patent prosecution costs; there are plenty of accidental discoveries that turned out to bring in a lot of revenue from very little development costs. The value of a patent is that it gives you an exclusive right to an invention. So the true value of a patent is the revenue it will allow you to bring in over its lifetime, from sale or licensing, or from litigation awards. Most companies also treat patent acquisition as an arms race: as long as you and your closest competitor both have big patent portfolios and are each infringing on the other's patents, and as long as patent litigation is as costly as it currently is, then you can have occasional skirmishes with out-of-court settlements being traded back and forth while avoiding an all-out infringement litigation war.
So, in neither case is a patent owner going to be enthusiastic about selling if a nonprofit shows up and says "we'd like to destroy your patent at the price of its development costs". To buy the patent, you'd have to cover the cost of anticipated revenue from that patent and the cost for having lost a deterrent against litigation.
Evidently you're not enough of a Lost fan to be justified in feeling betrayed. J.J. Abrams was no more responsible for season 6 of Lost than Stan Lee was for Spider-Man 3.
Oh great. It's tough enough for my introductory chem students to learn how to calculate the atomic mass of a molecule from its empirical formula when all the masses on the periodic table are single scalars. Using ranges for masses requires that they now have to add truncation, rounding, averaging, or some sort of consistent choosing to that process. They're screwed. And so is anyone who has to grade their papers (i.e., me).
Not necessarily. If you have prior art documents that would invalidate one or more of the claims, then you are more than welcome to file an ex parte reexamination request. That costs well less than millions of dollars.
And yes, the MPEP has been revised in light of KSR. On the other hand, Bilski is still up in the air because the Supreme Court is going to hear it next year. Believe me, there are a lot of us who want the Bilski dust to settle.
I've always found it sadly hypocritical that/. geeks who have so little patience with people making mistakes on technical issues, when said mistakes can easily be corrected by a little bit of reading, are comfortable making similarly blatantly wrong statements about the US Patent system, when said mistakes can easily be corrected my reading the freely available Manual of Patent Examination Procedure. I mean, seriously, nobody should spout opinions about patentability unless they've read MPEP 2100 through at least once. It's like trying to argue vi vs. emacs when the only text editor you've ever used is Notepad.
Okay, let me explain for you non-biochemist computer guys what this means. Take a computer, break it down into the smallest possible parts you can. I'm not talking about the hard drive/motherboard/case level. I'm talking about the level of transistors, resistors, ICs, connectors, motors, and the little blue LED that blinks whenever your hard drive spins. Now catalog everything. Keep a record of what you found where, and how many you found (eg, you found a laser in the DVD drive but not in the motherboard). So now you have a parts list, and a good idea of what parts to expect where. If you start finding unexpected things in unexpected places (like a SCSI connector on your video card, or an audio out port on one of your DIMMs), that tells you something is wrong.
Take a look at the database entry for something common like glucose. It's got
a brief, high-level description of the chemical
details about the chemistry
where it's found in the body
details about how much of it was found in what parts of the body based on various studies that have already been done
disorders it's linked to (eg, diabetes)
where to go for more information
Now what's missing is a lot of information about the connections, so technically this isn't really a map (because it's missing relational data), but a catalog. We need to know how each chemical turns into another, and what does the conversion. It's kinda like having a complete parts list for the computer, but not knowing how most of the parts fit together, nor how many volts and amps to run through the wires. Some of these connections we already know. I have a very large poster on my wall illustrating the more common chemical pathways in various organisms. It's not nearly as complete as this catalog in terms of chemicals, but it's got a lot of connections.
The connections are what's really useful. To continue the computer analogy, if you know that the blue LED connects to the hard drive, then if you don't see the blue light blink, then there's probably something wrong with the hard drive. A significant number of drugs aren't active in the form that you take them. They become active when the body (usually in the liver) converts them from the delivery form to the active form. But some people, because of their genetic makeup, convert the drugs differently. They turn them into different metabolites. These metabolites might be totally inactive, or even toxic in some cases. So if you know the connecting system, you can put a drug in, look for what metabolites result, and determine whether or not that person should continue taking the drug.
I have a friend in an MLS (masters of library science) program. She reports that it's about 90% female, and that other MLS programs around the US have similar percentages. It shouldn't be too hard for the/. crowd to figure out how to support that.
Believe it or not, there are a lot of CDs released outside RIAA. I'd like to see them try to claim ownership over that data.
Oh, who am I kidding. Yeah, they'll likely try.
I realize that the/. crowd is going to fellate any researcher who uses high-performance computing to draw pretty pictures, but from the Nature summary this sounds like a classic scientific case of showboating.
Not entirely, if you know the group and understand the context of the paper (which you apparently didn't read). They're from the UIUC group that develops NAMD, which is the MD program they used to do the simulation. So what they're demonstrating is not that they now know more about the STMV (the virus in question), because these guys are physicists and not molecular biologists. They don't care about how the capsid assembles. They know 50 nanoseconds isn't enough time to much more than the instrinic fluctuations of a single protein, let alone a huge structure. They do, however, care that NAMD is capable of handling huge MD simulations. The secondary results about STMV, such as the fact that the capsid alone is unstable without the RNA core, is just interesting material that bulks up the paper.
So I agree that probably the best thing to do would have been to release a technical communication saying "Hey, check this out! NAMD can handle a huge-ass simulation!" But they had just enough other information to turn it into a modest paper. And don't blame them for the fact that some other science editor saw the pretty picture (which their group does really well; I always use VMD for visualization because you can get some damn good pictures from it), skimmed the paper, and then wrote it up like it was the coolest thing ever.
And for heaven's sake, we're not officially reviewing their paper, so I call "attention whoring" on your anonymity.
I have a client who pulls out her cell phone every time she has a brain fart and calls me up to tell me about it. How do you measure that productivity?
I went to a really interesting lecture by David McCullough a couple of weeks ago. He spoke primarily about the context of the American Revolution. I found one of the most interesting points in his lecture to be one of his minor ones: in the 1700s, you couldn't send a message faster than anyone could physically travel, and even that was difficult. So it placed a large burden on people to make their own decisions with incomplete information. And superiors had to trust their subordinates, even to make huge and direction-of-the-country-changing decisions. McCullough said that the constant connectivity of today has its advantages, but can easily bring with it the drawback of superiors micromanaging their subordinates, and subordinates being incapable of making any decision on their own, especially with limited information.
So my friend was a pretty good Halo player. Good enough to win some local competitions. One night, his roommate's sister showed up with some of her friends. My friend and his roommate were playing, and after the round ended one of the girls asked if she could play against my friend. He patronizingly said, "Sure? You know how to play?"
"Well, it's been a while, but the controls should come back to me."
"Okay, I'll go easy on you for a bit."
Big mistake. I heard from everyone else in the room that by the time he hit 10 frags, she was already over 50.
Six months later they got married. He can usually win in Warcraft, but she still hands him his ass in any FPS.
So basically, the IDE/no-IDE argument is a rehash of the Safir-Whorf Hypothesis, just framed in programming terms. And just like the SF Hypothesis, it's still unresolved.
Since protein engineering is my field of study, for the benefit of the/. crowd (and my karma) I'll fill in the gaping holes left in the New Scientist article, and give you a little more background on the Nature paper. Because the writeup on/. is a perfect example of "scientific telephone": a semi-interesting result gets written up into a paper, which once it's been through several layers of editors suddenly seems like a major breakthrough.
The Nature paper isn't a breakthrough. It's not even really a major advance. Scientists in my field have been creating artificial proteins for five to ten years now. And yes, even some of them designed completely from scratch (though they're really simple; nothing as complex as, say, ATP synthase) instead of just taking a known fold pattern, known as a "motif." The "WW domain" (domain, in protein parlance, is a small, independent structure within a much larger protein---think of it like a module within the kernel or Apache) is a common fold in hundreds of different proteins. Basically, they analyzed the sequences of all of these WW domains, and figured out which positions were meaningful. It's kinda like reading through some code in a programming language you don't know, and figuring out which lines are comments and which lines are actual compilable code. This group found that the number of interesting positions is small, that they could identify them just from the amino acide sequence instead of having to mess with the whole complicated 3D structure of the domain, and that if they put together a protein with the meaningful amino acids intact and the non-meaningful positions randomized, then in many cases they could still get a pretty decent protein (in terms of structural similarity to the "natural" protein) out of it. Most of the paper is devoted to showing via various methods that they did get a pretty decent protein.
So what does this mean for me, assuming that this paper is absolutely correct (which I admit is a little hard for me to determine with one quick reading, given that I'm just a first-year grad student)? It means that the number of meaningful amino acids in a protein (at least in terms of overall structure) is pretty low, and that they can be identified without knowing what the full 3D structure is. This is good, because for a lot of proteins, the 3D structure is difficult to get. However, they picked an easy target: a small domain where there are over 100 unique sequences known. We'll see how well this method holds up with longer domains and fewer unique sequences. The S/N ratio won't be nearly as good.
And who raised the kids in such an attention-starved environment that they write to a handful (or more) of online entities just so they can feel some satisfaction and relevance in their lives? Seriously -- all the "deficiencies" of the younger generations that boomers bitch about now are a direct result of the self-centered, self-indulgent, self-everything lifestyle you guys fought so hard for back in the 60's. Now that it's biting you back, seems you don't want it anymore. Too late.
I was gonna say the same thing. I'm actually about to graduate with a BS in biochemistry, with an official minor in math and a de facto minor in CS (my school doesn't offer an official minor, but I've got the first 2.5 years of the CS major on my transcript). And next year I'm going into a biophysics PhD program, and planning to carry the computational experience with me.
So this is a great field to go into, provided you're actually interested in it. If all you want to do is increase your salary, then sell out and get an MBA. But if you want to do something really exciting (even if it does entail 5 years of grad school at a salary significantly lower than where you are now) and you're at all interested in biological/chemical sciences, then bioinformatics and systems biology is the way to go. Most large universities now have a program along these lines, and many are keen to bring in CS graduates. You'll have a significant learning curve during your first year getting caught up in molecular biology, cell biology, and biochemistry, but you'll bring an interesting and valuable perspective to the program.
Slashdot Mirror
Unfortunately there's no good way to define practicing versus non-practicing.
Not at all. A patent owner that really is trying to "promote the useful arts and sciences" is either trying to bring an implementation of the claimed invention to market, or is offering the patent for licensing. Virtually all patent trolls could be taken care of by requiring the plaintiff to show that they have made a good faith effort to do one of these two before they can bring a suit for infringement.
I went to the exhibit with the same question. One of the docents said that it was an engineering platform built for ground-based testing. There was an immense amount of ground-based testing and re-testing; failure of one of these satellites in orbit would have been a national security emergency.
This system already exists, and already functions better than it would if the USPTO were involved. If you want a patent to go into the public domain, do the following:
Not only does this procedure not need the involvement of the USPTO, but it has the added benefit of you not needing to pay any more for the patent than the selling price the owner is willing to accept.
On the other hand, determining the "selling price" is not quite as simple as "150% of the development costs". The value of a patent is not that it is a way of recouping your development and patent prosecution costs; there are plenty of accidental discoveries that turned out to bring in a lot of revenue from very little development costs. The value of a patent is that it gives you an exclusive right to an invention. So the true value of a patent is the revenue it will allow you to bring in over its lifetime, from sale or licensing, or from litigation awards. Most companies also treat patent acquisition as an arms race: as long as you and your closest competitor both have big patent portfolios and are each infringing on the other's patents, and as long as patent litigation is as costly as it currently is, then you can have occasional skirmishes with out-of-court settlements being traded back and forth while avoiding an all-out infringement litigation war.
So, in neither case is a patent owner going to be enthusiastic about selling if a nonprofit shows up and says "we'd like to destroy your patent at the price of its development costs". To buy the patent, you'd have to cover the cost of anticipated revenue from that patent and the cost for having lost a deterrent against litigation.
Evidently you're not enough of a Lost fan to be justified in feeling betrayed. J.J. Abrams was no more responsible for season 6 of Lost than Stan Lee was for Spider-Man 3.
Oh great. It's tough enough for my introductory chem students to learn how to calculate the atomic mass of a molecule from its empirical formula when all the masses on the periodic table are single scalars. Using ranges for masses requires that they now have to add truncation, rounding, averaging, or some sort of consistent choosing to that process. They're screwed. And so is anyone who has to grade their papers (i.e., me).
Not necessarily. If you have prior art documents that would invalidate one or more of the claims, then you are more than welcome to file an ex parte reexamination request. That costs well less than millions of dollars.
/. geeks who have so little patience with people making mistakes on technical issues, when said mistakes can easily be corrected by a little bit of reading, are comfortable making similarly blatantly wrong statements about the US Patent system, when said mistakes can easily be corrected my reading the freely available Manual of Patent Examination Procedure. I mean, seriously, nobody should spout opinions about patentability unless they've read MPEP 2100 through at least once. It's like trying to argue vi vs. emacs when the only text editor you've ever used is Notepad.
And yes, the MPEP has been revised in light of KSR. On the other hand, Bilski is still up in the air because the Supreme Court is going to hear it next year. Believe me, there are a lot of us who want the Bilski dust to settle.
I've always found it sadly hypocritical that
Okay, let me explain for you non-biochemist computer guys what this means. Take a computer, break it down into the smallest possible parts you can. I'm not talking about the hard drive/motherboard/case level. I'm talking about the level of transistors, resistors, ICs, connectors, motors, and the little blue LED that blinks whenever your hard drive spins. Now catalog everything. Keep a record of what you found where, and how many you found (eg, you found a laser in the DVD drive but not in the motherboard). So now you have a parts list, and a good idea of what parts to expect where. If you start finding unexpected things in unexpected places (like a SCSI connector on your video card, or an audio out port on one of your DIMMs), that tells you something is wrong.
Take a look at the database entry for something common like glucose. It's got
Now what's missing is a lot of information about the connections, so technically this isn't really a map (because it's missing relational data), but a catalog. We need to know how each chemical turns into another, and what does the conversion. It's kinda like having a complete parts list for the computer, but not knowing how most of the parts fit together, nor how many volts and amps to run through the wires. Some of these connections we already know. I have a very large poster on my wall illustrating the more common chemical pathways in various organisms. It's not nearly as complete as this catalog in terms of chemicals, but it's got a lot of connections.
The connections are what's really useful. To continue the computer analogy, if you know that the blue LED connects to the hard drive, then if you don't see the blue light blink, then there's probably something wrong with the hard drive. A significant number of drugs aren't active in the form that you take them. They become active when the body (usually in the liver) converts them from the delivery form to the active form. But some people, because of their genetic makeup, convert the drugs differently. They turn them into different metabolites. These metabolites might be totally inactive, or even toxic in some cases. So if you know the connecting system, you can put a drug in, look for what metabolites result, and determine whether or not that person should continue taking the drug.
I think he's quite content knowing that his microhero status is still architectually superior.
That's only the lecture portion, it's boring as hell, and you don't learn anything useful anyway. The lab sections are where it's at.
You've got one level left: Temple.
I have a friend in an MLS (masters of library science) program. She reports that it's about 90% female, and that other MLS programs around the US have similar percentages. It shouldn't be too hard for the /. crowd to figure out how to support that.
... for screwing around with a 15 year old. For the last nine years.
Believe it or not, there are a lot of CDs released outside RIAA. I'd like to see them try to claim ownership over that data. Oh, who am I kidding. Yeah, they'll likely try.
Wish I could figure out why I can't get it to use my custom MP3's as "ringtones" but that's not exactly an important feature for me.
Check out Moto4Lin. I've got a V-188 too, and I've uploaded custom ringtones and backgrounds onto my phone using it.
I realize that the /. crowd is going to fellate any researcher who uses high-performance computing to draw pretty pictures, but from the Nature summary this sounds like a classic scientific case of showboating.
Not entirely, if you know the group and understand the context of the paper (which you apparently didn't read). They're from the UIUC group that develops NAMD, which is the MD program they used to do the simulation. So what they're demonstrating is not that they now know more about the STMV (the virus in question), because these guys are physicists and not molecular biologists. They don't care about how the capsid assembles. They know 50 nanoseconds isn't enough time to much more than the instrinic fluctuations of a single protein, let alone a huge structure. They do, however, care that NAMD is capable of handling huge MD simulations. The secondary results about STMV, such as the fact that the capsid alone is unstable without the RNA core, is just interesting material that bulks up the paper.
So I agree that probably the best thing to do would have been to release a technical communication saying "Hey, check this out! NAMD can handle a huge-ass simulation!" But they had just enough other information to turn it into a modest paper. And don't blame them for the fact that some other science editor saw the pretty picture (which their group does really well; I always use VMD for visualization because you can get some damn good pictures from it), skimmed the paper, and then wrote it up like it was the coolest thing ever.
And for heaven's sake, we're not officially reviewing their paper, so I call "attention whoring" on your anonymity.
I have a client who pulls out her cell phone every time she has a brain fart and calls me up to tell me about it. How do you measure that productivity?
I went to a really interesting lecture by David McCullough a couple of weeks ago. He spoke primarily about the context of the American Revolution. I found one of the most interesting points in his lecture to be one of his minor ones: in the 1700s, you couldn't send a message faster than anyone could physically travel, and even that was difficult. So it placed a large burden on people to make their own decisions with incomplete information. And superiors had to trust their subordinates, even to make huge and direction-of-the-country-changing decisions. McCullough said that the constant connectivity of today has its advantages, but can easily bring with it the drawback of superiors micromanaging their subordinates, and subordinates being incapable of making any decision on their own, especially with limited information.
So my friend was a pretty good Halo player. Good enough to win some local competitions. One night, his roommate's sister showed up with some of her friends. My friend and his roommate were playing, and after the round ended one of the girls asked if she could play against my friend. He patronizingly said, "Sure? You know how to play?"
"Well, it's been a while, but the controls should come back to me."
"Okay, I'll go easy on you for a bit."
Big mistake. I heard from everyone else in the room that by the time he hit 10 frags, she was already over 50.
Six months later they got married. He can usually win in Warcraft, but she still hands him his ass in any FPS.
All sysadmins who are still running this insecure setup are advised to patch your systems immediately. Yes, all fourteen of you.
So basically, the IDE/no-IDE argument is a rehash of the Safir-Whorf Hypothesis, just framed in programming terms. And just like the SF Hypothesis, it's still unresolved.
Since protein engineering is my field of study, for the benefit of the /. crowd (and my karma) I'll fill in the gaping holes left in the New Scientist article, and give you a little more background on the Nature paper. Because the writeup on /. is a perfect example of "scientific telephone": a semi-interesting result gets written up into a paper, which once it's been through several layers of editors suddenly seems like a major breakthrough.
The Nature paper isn't a breakthrough. It's not even really a major advance. Scientists in my field have been creating artificial proteins for five to ten years now. And yes, even some of them designed completely from scratch (though they're really simple; nothing as complex as, say, ATP synthase) instead of just taking a known fold pattern, known as a "motif." The "WW domain" (domain, in protein parlance, is a small, independent structure within a much larger protein---think of it like a module within the kernel or Apache) is a common fold in hundreds of different proteins. Basically, they analyzed the sequences of all of these WW domains, and figured out which positions were meaningful. It's kinda like reading through some code in a programming language you don't know, and figuring out which lines are comments and which lines are actual compilable code. This group found that the number of interesting positions is small, that they could identify them just from the amino acide sequence instead of having to mess with the whole complicated 3D structure of the domain, and that if they put together a protein with the meaningful amino acids intact and the non-meaningful positions randomized, then in many cases they could still get a pretty decent protein (in terms of structural similarity to the "natural" protein) out of it. Most of the paper is devoted to showing via various methods that they did get a pretty decent protein.
So what does this mean for me, assuming that this paper is absolutely correct (which I admit is a little hard for me to determine with one quick reading, given that I'm just a first-year grad student)? It means that the number of meaningful amino acids in a protein (at least in terms of overall structure) is pretty low, and that they can be identified without knowing what the full 3D structure is. This is good, because for a lot of proteins, the 3D structure is difficult to get. However, they picked an easy target: a small domain where there are over 100 unique sequences known. We'll see how well this method holds up with longer domains and fewer unique sequences. The S/N ratio won't be nearly as good.
I think all the scientists at the NIH and the NSF would beg to differ.
And who raised the kids in such an attention-starved environment that they write to a handful (or more) of online entities just so they can feel some satisfaction and relevance in their lives? Seriously -- all the "deficiencies" of the younger generations that boomers bitch about now are a direct result of the self-centered, self-indulgent, self-everything lifestyle you guys fought so hard for back in the 60's. Now that it's biting you back, seems you don't want it anymore. Too late.
Hey, do you have a source for this statement? I've got a friend that's a hard-core anti-gun freak, and I'd like to have some info against him.
I was gonna say the same thing. I'm actually about to graduate with a BS in biochemistry, with an official minor in math and a de facto minor in CS (my school doesn't offer an official minor, but I've got the first 2.5 years of the CS major on my transcript). And next year I'm going into a biophysics PhD program, and planning to carry the computational experience with me.
So this is a great field to go into, provided you're actually interested in it. If all you want to do is increase your salary, then sell out and get an MBA. But if you want to do something really exciting (even if it does entail 5 years of grad school at a salary significantly lower than where you are now) and you're at all interested in biological/chemical sciences, then bioinformatics and systems biology is the way to go. Most large universities now have a program along these lines, and many are keen to bring in CS graduates. You'll have a significant learning curve during your first year getting caught up in molecular biology, cell biology, and biochemistry, but you'll bring an interesting and valuable perspective to the program.
... about as valid as my [a biochemist's] view on optics. Just 'cuz you've got a MS in one field doesn't make you an expert in another.