GDG

They disperse in a vacuum; not in selected nonlinear optics. Apparently useful for keeping pulses separate (rather than spreading and overlapping) in high bit-rate fiber optic transmissions.

It passes through: it just leaves a hole behind

Sorry, but 10% of a survey sample saying they want something is not the same as 90% saying it is a bad idea. You could easily have 50% saying "not sure", and 35% saying "I don't understand the question".

If your activity involves affinity to a target, fix your target on a plate (or other substrate), add a pool of your glycoforms in solution, equilibrate, and see which glycoform binds to the substrate most.

I don't think you'll find any disagreement with the idea that there was liquid water present prior to the emergence of life on Earth. In fact, even biblical Creationists would agree with that one. Since every living thing on the planet is based on aqueous chemistry, I think most of us accept the prior existence of water as a given. What I don't understand is why you think this is such a mystery

You've obviously never used a cutting laser. According to the EPA, nuclear subs use "steel, water tanks, and polyethylene" for radiation shielding. Probably weighs a lot less than lead (and having less mass makes the sub more manuverable).

Stem cells mainly differentiate into other cells, depending on their environment. If they differentiate into osteoblasts, they'll make bone (and if they differentiate into osteoclasts, they will dissolve/remodel bone).

You can have optical solitons, but the effect depends on the medium.

Yes, there have been significant advances in treating cancer over the past few decades. However, it is not as simple as all that. First off, cancer is typically not the result of a single gene gone haywire: there are a number of checks that have to be circumvented before the cell becomes neoplastic. For example, the cell has to lose contact inhibition, lose cell cycle regulation, and has to overcome the p53 program that causes apoptosis if there is a problem in replication. Frequently, tumor cells also secrete angiogenic factors to induce blood vessel formation (otherwise they starve), and tumors that become metastatic must also express the proteins that allow them to pass through blood vessel walls and into the circulatory system (and back out again). Also, tumor cells do not necessarily express a unique marker protein. Consider where those proteins have to come from: they are all already encoded in the normal patient's genome. You may find that the surface protein that characterizes the tumor also characterizes certain other normal cells. Plus, targeting that surface protein (even when it is essentially unique, e.g., it is a fetal antigen not normally expressed in the adult) can drive selection of tumor cells that do not express the antigen. It sometimes happens that the tumor shrinks by half, and then comes back when the cells that were not expressing the antigen proliferate and take over. Unfortunately, cancer is something that could easily keep up busy for decades to come

Happy to help. Have my own SF novel simmering on the back burner... BTW, the CDC has a free monthly publication called Emerging Infectious Disease that you might find helpful.

In my experience, this is relatively rare. If it is difficult to manufacture, it just costs more. Obviously, nothing that cannot be synthesized ever gets tested A typical drug discovery program first settles on a molecular target: e.g., a receptor, a cytokine, an enzyme essential for a pathogen's survival or spread, etc. Compounds that interact with the target are designed or identified. If successful drugs for that target are already known, new drugs may be designed by comparing the morphology of several successful drugs. Otherwise, one can identify potential leads by screening compound libraries or fragment libraries for anything with activity. Then, more compounds are designed based on the screening results. After several compounds having activity are made and tested in vitro, further variations are designed and synthesized in an attempt to increase the activity (and/or reduce side effects and undesireable properties, like rapid excretion or metabolism). Each lead may result in a group of several hundred or thousand compounds having a related structure. Likely candidates are selected from those groups, and are tested in animals. Due to the expense of conducting trials, typically only 1-3 compounds are selected for preclinical trials. The compounds that were not selected are not discarded, but are added to the company's compound library, where they will get screened periodically for activity against other targets. Merged post follows: Consecutive posts merged Well, this is the hard part. Your body has a large set of enzymes that metabolize foreign compounds. Some enzymes look for aromatic rings, and oxidize their substituents. Others latch onto free OH groups and attach a glucuronic acid group. Frequently, these modifications destroy the activity of the drug, and/or cause it to be rapidly removed from the system. In some cases, it is possible to substitute another substituent for the group that was affected. Sometimes, the new group simply activates a different enzyme, and there is no net gain. Sometimes, it turns out that the group is essential to the activity of the drug, and there is no way to replace it while maintaining activity. In other words, sometimes it is simply not possible to prevent the drug from being modified by "body chemistry." In such cases, one generally starts over with compounds having a different basic structure. There are a few compounds that specifically inhibit particular CYP enzymes. However, we did not evolve CYPs just to make it difficult to design drugs: these enzymes are required for your basic metabolism and deactivation of toxins found in the environment (and in your food). Knocking out CYPs so that your drugs work is likely to cause more problems than it solves (acceptable only in life-or-death situations).

I recommend searching on PubMed: most medical information that is published will be cited there, and you can search the abstracts. Some of the journals also provide free access.

And let's not forget that waves can be caused by a sudden vertical displacement in bottom of the container (or sea floor)...

Gelatin is essentially denatured collagen, which is the main structural protein found in connective tissues and cartilage in all animals. If the microbes are not pathogenic, perhaps they are digesting proteins released by animals (e.g., mucus, sloughed skin, etc.) or decomposition. My guess is that you would also find gelatinase expressed in microbes that are responsible for curing meats.

While it is obviously true (to us, at least) that TB and HIV do not "merge", there is a substantial problem with co-infection. I'm guessing he heard somebody discussing the March 2009 issue of Lancet Infectious Disease, e.g., A. Zumla et al., Lancet Infect Dis (2009) 9(3):197-202 "Reflections on the White Plague" M.J. Reid and N.S. Shah, Lancet Infect Dis (2009) 9(3):173-84 "Approaches to tuberculosis screening and diagnosis in people with HIV in resource-limited settings"

A few ideas: Having an insect vector means that the main focus for controlling the plague will be vector control, i.e., spraying the mosquitoes, wearing protective garments, etc. Also, likely that this will be a much bigger problem in the developing nations than in the developed world -- cf. malaria, etc. Your best and fastest epidemics are usually spread directly, human to human. Are you sure you want the cure present in spit? You might be able to get more drama out of the situation if the cure is in their blood: Frank_sub slowly retreated from the mob, until he reached the wall and could go no further. Arthur, in front, coughed wetly into his sleeve, and wiped the blood away on the back of his hand. "Now, Frank_sub, we don't wanna hurt ya. We just need ya to spit inta this cup here." OR "Frank_sub slowly retreated from the mob, until he reached the wall and could go no further. Arthur, in front, coughed wetly into his sleeve, and wiped the blood away on the back of his hand. "Now, Frank_sub, we don't wanna hurt ya. We just need a little bit o' your blood..." If the Subs have been engineered to express the cure protein, then it will also be no problem to manufacture the protein. It is possible to culture human cells, and collect the protein. Could be expensive, but not impossible. If the Subs express the protein, you'll also have to think of a reason why gene therapy won't work on the normals. This would be a natural solution, if it would work, and there would be great incentive to make it work... Short proteins (oligopeptides) can be made chemically. Longer proteins are usually expressed recombinantly in a host cell. When a mammalian protein is expressed naturally, it is often subject to post-translational modification. This can be adding carbohydrate (sugar) molecules to certain parts of the protein (a process called "glycosylation"), or lipids or other molecules, cross-linking parts of the protein (typically by disulfide bonds), cleaving parts of the protein, etc. The way that the linear polypeptide chain folds up to make a functional protein can be critical. If the protein doesn't fold right, it is "denatured" or misfolded, and won't have the correct activity (it may have no activity at all). When proteins are expressed recombinantly (i.e., in a host other than the original source of the protein/gene), you can encounter problems. If you express a mammalian protein in bacteria (E. coli is a favorite host), no glycosylation occurs. For some proteins, this is not a problem (and some proteins just are not glycosylated to begin with), but for others, it can affect how long the protein lasts in the body, and in some cases glycosylation is essential for activity of the protein. If you express the protein in yeast, you'll get glycosylation, but it will usually be somewhat different from the native glycosylation pattern (yeast may use different types of sugar, and may add more or less sugar than the native form). Expression in mammalian cells is the most difficult and expensive, but is definitely doable on a commercial scale. I can't think of a scientific reason why it would be impossible to manufacture the cure protein if the Subs can express it naturally. Even if you postulated that the Subs have a new and different glycosylation pathway (which would require a huge effort, because nearly every protein in the body would require some redesign), manufacturers would simply use cell cultures of Sub cells for manufacturing. Even if the cure protein is previously unknown, it is only going to be an obstacle for a matter of weeks or months (much less time than it would take to design and raise the Subs). Suppose the Subs were created for a different purpose, and just happened to be immune to the Grip. And suppose that it was later discovered that a protein in Sub saliva functioned as a cure. Presumably, researchers would know how the Subs were changed genetically, and one of those changes would be responsible for the cure. Not too many things to check. Even if all of the records had been lost or suppressed, Researchers would collect saliva samples, and examine the proteins contained in the samples by gel electrophoresis (this is a lab technique that separates proteins based on their electrical charge and size). If there were only one or two proteins in Sub saliva not found in "normal human" saliva, that would be your dead giveaway. Scientists would extract and purify more of that protein, and test it against the pathogen. It is not too difficult to sequence part of the protein, and the probe the genome or a cDNA library for the likely gene that encodes the protein. Even if the cure protein was only an altered form of an existing protein, there are not too many proteins in saliva: researchers would simply test each fraction for activity against the pathogen until they identified the responsible protein. Likely to take a matter of a few weeks to identify the protein, and several months to start manufacturing commercial-size quantities. However, the biotech/pharmaceutical industry as a whole probably does not have the capacity to make enough of any kind of protein to treat the global population, if the disease is pandemic. Perhaps that is your solution: the protein can be manufactured, but not quickly enough to get it to everyone. Or perhaps manufacture is controlled or suppressed or sabotaged by some group of evil-doers.

Yes, there are many charged particles in space. See for example the Van Allen Belts.

Sure, this is possible, although I don't know of any examples. Some enzymes are proteases, which means that they cleave a protein into smaller bits. Most proteases are specific for a particular amino acid sequence, meaning that they will only cut certain target proteins, and only at a particular place in the protein sequence. There are many examples of proteins that are expressed in an inactive form, which become active only after a protease removes part of the protein. For example, insulin is expressed as a single amino acid chain, which is inactive. A protease clips out a section of the middle of the sequence, leaving the two ends bound together: that is the active form. In some cases, the protein that gets activated is itself a protease, which goes on to activate still other proteases, and so on. The coagulation system and the complement system are two other examples. You should really read up on biology -- it is fascinatingly complex. So it is conceivable that your subspecies (or uberspecies) could have an enzyme that hydrolyzed (cut) part of the grip virus capsid, and thereby prevented it from binding to cells. Of course, as soon as this fact was recognized, that enzyme would become the cure: pharmaceutical companies would simply manufacture the enzyme, for intravenous injection. Instant cure. You'd have to set it up so that the subspecies enzyme also cleaved an essential "normal human" protein, so that it would be unusable for the rest of the population. Perhaps it would activate the clotting cascade, so that a normal human's entire circulatory system would clot up instantly upon administration Could be a good plot development point

a.) AFAIK, the Scharnhorst effect applies only to photons, not matter (and in a Casimir gap, it is virtual particles that are excluded). Material objects are not absorbed by virtual particles and re-emitted, so we don't expect any velocity increase in a Casimir gap. b.) You are not going to be able to accelerate any material object to the speed of light in a 3 km conduit. Consider what kind of acceleration would be required

Basically, you won't be able to detect any variation in intensity that oscillates faster than around 80 Hz (probably a bit less, actually). You would see it as unvarying.

http://en.wikipedia.org/wiki/Virus#DNA_viruses Merged post follows: Consecutive posts merged NB: not all RNA viruses are retroviruses

I think the field of Biology has gone much further than you are aware. You would probably find a good textbook (or even a course) on general biology to be fascinating, and well worth your time Can anyone suggest a good general bio book to get him started? Note: when considering a biology book, steer clear of those that argue that evolution is "only a theory": they will lead you astray. Evolution is a theory in the same sense that quantum mechanics is: it is the best scientific explanation we have for the way the world works. Although scientists still differ on some of the finer points, like details of mechanism, no serious biologist doubts that evolution is the way that complex organisms arise. Books that attack evolution, or purport to offer a "balanced approach" invariably leave out or misstate the facts.

For that matter, not all 3D terrestrial critters have separate orifices for ingestion and elimination. Some are more of a sack, morphologically.

I don't recall running across that specific term before, but it has been well known for some time that cells have "housekeeping" functions to maintain their homeostasis. Cells continually make new proteins (and other molecules) to replace those that have been damaged (or have been tagged for autophagy). I would be very surprised if it had anything to do with consciousness or cognition.

I don't know if there has been a scientific study of the question, but here are the factors that I would guess go into it: Nursing is an investment (and substantial energy drain) for the mother, requiring the mother to eat and drink more than she would otherwise need. Thus, weaning as early as possible is best for the mother. However, it takes some time for the neonate's digestive system to be ready for "regular food". For example, the digestive tract is typically colonized with bacteria (some of which aid in digestion), the jaws and teeth need to mature to some point, etc. Milk provides a high-calorie, easy to digest food until the newborn's digestive system is ready. Given that, my guess would be that weaning occurs when the child has developed to the point where it can digest food other than milk. In humans, my guess is that the coordination necessary for chewing and swallowing solid food is the rate limiting step. In cows, probably the colonization of the rumen.