CharonY

I am still a bit unsure what new things this law actually provides. One this is apparently that during lawful stops etc. the ID and immigration status can be checked. But couldn't they do it before already? The only thing in this regard that I could think of is that they may also query those directly/indirectly involved. For instance during a car stop they may also check the immigration status of the passengers. On politifact they also mentioned that e.g. an unkempt lawn or similar may trigger such a check as it would be during enforcement of local laws. The other thing is that all immigrants now have to carry their papers with them and that apparently the officer now is to required to check in case of suspicion. It leaves enough wriggle room (I think) that it is unlikely that the police is not easily sued for not checking, but who knows? Edit: apparently there is some more around on politifact. Gotta read it when I got a time slot http://www.politifact.com/truth-o-meter/article/2010/apr/28/arizona-immigration-law-fact-checked/

Actually samples from diseases patients are generally more interesting.

The Rubik cube is not a fitting analogy as it implies one final structure that has to be reached actively. Protein folding is dynamic and usually self-organizing, however (requiring interactions within proteins as well as between protein and solvent). Essentially for each medium condition the protein will acquire the most stable thermodynamic state spontaneously. In some cases this is not necessarily the active form though. Algorithms involved in modeling (which is more accurate than "solving") protein structures essentially calculate interactions between the residues in a given medium and thus determine the most likely state. Again, code solving or pattern detection is not a good analogy to describe that. It is more like making a huge amount of thermodynamic calculations. For the most part the interactions are well known, but the challenge is the sheer amount of individual interactions and cross-interactions. However, the final state is defined. The role of chaperones is generally to overcome energy barriers and guide the fold into the active form (if they cannot reach it spontaneously) , or, if several stable states exist, it serves to acquire a specific one. It has little to do with being crowded or not (although in specific cases there may be modulations due to whatever is around).

Well, that would be the short answer.

If there was a discussion at all. If it is too strong of crap many scientists try not to touch it. There would have been a larger outcry if that was presented in a well-known science journal.

I am not too familiar with the the law making process here, however weren't those that were accused of not having read the health care bill actually voting on it, whereas in the case of Arizona's law are not? I do agree that it is cheap to comment on something that one does not know the details of, though.

De novo design tends to utilize folds found in nature and thus are often not completely artificial. However, using protein models one they can have totally different sequences. Proteins require the correct medium in order to fold properly and often also require additional factors besides the solution (e.g. chaperones or co-factors).

How is that supposed to work? And what do you mean with nitrogenous? Nitrogen fixing (N2 to NH3)? Or Nitrate reducing (NO3- to NO2-). And how to do you propose to use it for an engine?

So mass media are alarmist. Who would have guessed. You are aware that that is not part of the mainstream global warming models? In fact, I would be surprised to find any significant amount of publications on that matter. Well, after reading the page I failed to find the bibliography for this kind of "resrarch". And more about it http://wattsupwiththat.com/2010/05/18/most-idiotic-global-warming-headline-ever/ OK question. Who are "they"? Newspapers? Bloggers?

I am wondering what offences not involving murder would result in life sentences for children.

a) how about using normal fonts? b) it is standard procedure to cultivate them on feeder cells where they exhibit undifferentiated proliferation.

Well said, spin. And much more concise. For some reason the more tired I get, the more verbose I become. And randomness of punctuation increases.

Nope. The main reason is that the amount of graduates as increased dramatically, whereas the number of tenure positions remain almost the same (or had a far lower increase). Also you cannot just be an assistant prof. Because after five years you get a tenure review and if do not get tenure, you are out. Problem is that by then you may be around 40, and if you do not have good contacts in another track, you are in deep trouble. Just something to keep in mind. Academia has more and more become a high risk track. Of course, people still succeed, but it takes much more strategic planning and commitment to the career (as opposed to merely doing science). Just doing good or even great science alone is insufficient nowadays (unless you get really lucky). In other words, if you really want to get an academic career plan early, and realize what it really takes to get it. Also, ask younger faculty for advice (around the time you are in a PhD program) as they are more likely to have more personal experience with the new reality of academic careers than the old big-shot profs. There is a reason why many start their PhD fully expecting to run a research group in some top university but instead decided to get a job in industry or started a teaching career.

How about another, more simple reason. How do you nail down the result of multifactorial processes as e.g. ulcers down to a single source? This is also somewhat true for the growth question. Even within a tissue cells are not identical. Thus if only a very limited amount of these cells do exhibit growth, it is simply not easy to detect. In fact, it is known that certain neurons do indeed exhibit limited growth. It is, however not rapid growing and proliferating as in other tissues and it thus took a while to demonstrate that. Bottom line is that especially as we cannot conduct invasive and harmful experiments on humans, we have to rely on high-dimensional epidemiological data or animal models that may or may not apply to humans to find associations of some stimuli with certain effects. But as no everyone reacts the same to the same stimuli many of these findings will likely to be invalidated eventually, unless a a specific mechanism exists that can be identified.

So you want to be a researcher? Which level? I am not sure what tracks exist in this field, however if you want an academic career, you should be prepared to realize that positions are very limited. The reason is that normally staying in academia usually requires tenure eventually. Statistically only around 20% of all PhDs in academic track will eventually reach it. You should inform yourself how academic careers look like (it requires far more than "mere" research) and whether if you want to give a shot at it. Also be prepared to have a second track in the real world that you can start, if the academic track fails. In any case, if you want to get into academic, usually a PhD is required. If bench work is really what you are after, however, you can also be a technician. That usually does not require a PhD and you can do more labwork (most at the level of assistant prof or higher rarely have time to do effective labwork themselves).

I would turn the question around and ask, what do you want with a master or a PhD? Just the enjoyment of learning something or do you plan to have a science career? And if so, what kind of career? Usually it is better to envision where you want to end up, rather than only looking at the proximate steps.

I can assure that wordy writing will get you a bad paper review (I get enormously fed up when I review one). And it is far worse for grant reviews. If anything, the trick to getting published or funded is doing the inverse. Well, that and being well-known and connected in your field Edit: I am talking about natural sciences, though.

It depends precisely on what you are seeing and your extraction protocol. Are the additional bands on the height of the 16S rRNA?

The identification of own cells requires quite not only the presence of subject specific antigens, but also the absence of foreign ones. So in effect you would have, on the molecular level, recreate the surface structure of a cell perfectly on the substrate you want to introduce. Plus, it has to be perfectly stable and may not, interact in any way and give rise to anything foreign that the immune system may detect. This involves far more than putting protein on top of it (even considering highly complex glycoslyation patterns). Right now, to my knowledge there is not even a theoretical approach for that. And Biohacking is such an absurd word.

Seconded. Depending on the type of PCR and the way of storage a year old DNA can yield lousy results. Of course, the remaining components should also be relatively fresh.

*sigh* that is why I hate those uninformed silly posts. Those without sufficient knowledge in the field could take them seriously. Almost all biomolecule analyses take the (aqueous) medium into account. It is neither groundbreaking or underfunded (well, which branch isn't?) but it is common knowledge. Depending on the type of interaction additional parameters as ion strength, pH (surface charges) etc. are also part of it. The interaction is far more complex than simply hydrogen bonds. Also common knowledge. The DNA part is utter nonsense. There is course well-known data on how the helix twist change in dependent on the ionic strength of the solution, though. I have to add that designing novel artificial proteins are (to my knowledge) only met with moderate success. Those in use tend to be modified proteins (e.g. adding linkers or anchors) rather than de novo structures. But this is not really my specialty.

No, selective pressure are expected to vary dramatically from population to population (even within a species). Selective advantages of altruism have been well investigated. Vampire bats are the classical example.

Excuse me, but do you even try to make sense?

A) studies have shown that coffee is not significantly more diuretic than other drinks (e.g. water). Caffeine alone has no obvious diuretic properties (up to normal consumption levels). B) if you are talking about cups of coffee (as opposed to highly concentrated caffeine levels) then 10 cups are not acutely dangerous, though possibly unhealthy over a long time. The oral LD50 is around 192 mg/kg weight. Assuming a weight of, say 70 kg it would be around 13.44 grams. That would roughly require drinking around 100 cups in short time (without excretion). That is about 12.5 l. Even I would have trouble getting that much coffee in within a day, even disregarding elimination from the system. What Stacie proposes makes a lot of sense, but I would have to look up details.

I am not sure where the problem is. It requires as an input the averaged difference in allele size squared. See also the reasoning here: SLATKIN, M. 1995. A measure of population subdivision based on microsatellite allele frequencies. Genetics 139: 457–462. I am not sure whether there is a tool out there doing all the formatting for you, though. Relatively few but popular tools get third-party add-ons.