CharonY

Heh? Why use bleach if ether denatures proteins perfectly?

As participant in epidemiological studies perhaps?

It depends on what kind of electrophoresis you are doing. For proteins generally polyacrylamide gels are used instead of agarose. The reason why SDS is used is easily answered. In order for gel electrophoresis to work all the particles should have roughly similar charges (at least no inveresd polarity). Think about proteins, is that the case? For some other specialized applications SDS can have other uses including cell lysis in-gel.

Well, yeah, phagocytes are producing them in peroxisomes and they are part of plants self defence against bacteria, too. There are also some more exotic reactions that require H2O2 in low amounts, but drinking it would not benefit either effect. Baseline is that ROS have to be controlled within cells and lack of it is one of the reasons why some organisms cannot stand oxygen.

In the simplest and most common case, receptor binding is an equlibrium reaction. In other words, molecules bind to the receptor and get released constantly. This reaction is not timed. I.e. at any given time point there is a certain equilibrium of free and bound transmitters. The rate is determined by the affinity of the molecule to the receptor. How much is bound at any given time in a population of receptors is determined by the concentration of the molecules and the amount of receptors present (also see law of mass action). Temperature jiggling is a strange way to describe Brownian motion.

Be frank and do not waste her time.

While the Q is addressed to skeptic I will provide some quick answers. 1) No benefit is gained, the disproportionation is a defensive mechanism. Under normal conditions H2O2 is accidentally formed during respiration. Mostly due to leaking of electrons out of the ubiquinon pool. 2) H2O2 belong to the family of reactive oxygen species. It is especially involved in the Fenton reaction which generate extremely harmful hydroxyl radicals that readily react with about anything. This leads to DNA and protein damage, among others and harm the cell about anywhere it encounters it. To make it short, your body makes a good effort to prevent you from creating these nasty buggers. It is a bad idea to intentionally flood it with it. I recommend reading up on oxidative stress, ROS and Fenton reaction for this topic.

Now, now. At no need to get personal. At the very least he did not do it (hopefully) before asking. Although a forum is a VERY weird to ask as opposed to, say, the supervisor or other (senior) students. In addition it appears that there was either a very bad safety instruction, or (another common occurence) a sudden loss of common sense when entering a lab. Cooking gasoline at home is probably something that hardly anyone could come up with. However, most autoclaves won't blow up. The most likely scenario is that you will have a room full of ether and an autoclave with a shattered bottle. If there is some fire starter nearby it could get worse from there, though. It is also bad if it does not explode within the autoclave, though. If you pull out the bottle while it is still under pressure from the ether and it did not explode until then, it may well very happen shortly after you open the autoclave (and release the pressure) . In that scenario you have all the above plus a face full of shards.

Heh, that was what popped into my mind first thing, too.

Do not, I repeat, do not autoclave volatile compounds and do not close the bottle tightly. Think for a sec what is going to happen. Evaporation is the smallest of your probs. Also, how likely is contamination of ether?

Actually it is not an enhancement of growth, but rather a reduction in presence of CO2 (5% and above). I think it was mainly Pseudomonas aeruginosa and some non-specified Enterobacteriaceaethat got inhibited, presumably due to a decrease in pH. It was based on a old study in the 80s and I am not sure whether it got updated. I am only aware of clinical stool isolates that were obtained under ambient conditions.

Well, chemical weapons generally have a much more localized impact than nuclear (if considering the radiation, fallout, etc.). Biological weapons are, as already mentioned, much less proven. There are a number of issues for effective bioweapons. Just consider the anthrax affair a while back. The main reason why bioweapons are feared are the (either perceived or real) lack of control over them once released. Bioweapons are more likely to be a greater threat to underdeveloped countries with little access to health care. Considering that, the most effective way to deploy them in a developed country is first to ruin the health care system (or make it so expensive that only a small elite can afford it) so that once a disease appears it spreads around. Also inciting fear of vaccines may help.

There are a number of enzymes protecting from reactive oxygen species, among them a couple in the family of peroxidases. However it is catalase (also a member of that family) that converts H2O2 to water and oxygen. The enzymes actually termed peroxidases result in H2O and an oxidized donor. A basic enzyme for oxidative stress response is the gluthathione peroxidase. The net result is 2H2O and oxidized glutathione.

Drink H2SO4!!! It has double the oxygen than O2!!!!!!! Seriously, that has to be one the dumbest scams around.

As most are equlibrium reactions, you would also to have to remove the product from the system, otherwise upon reaching equilibrium no further net reaction is going to happen. Otherwise it depends on the stability of the protein on how long it can continue working.

It depends on the program and availability of funds. However, if you can clearly communicate what you did and have the papers to back them up (the first part is more important, though, as I had couple of times grad students with papers but no idea about what they have been supposedly written), you should be fine. Grades are mostly (though some may disagree) to distinguish those that have nothing else to show up for. Submit a focused application (i.e. achievements vs everything what you have done), and try to get to talk to the respective PIs directly. As in any other job search, networking will always provide you with an edge.

If you manage to create a working ecosystem on a microsclide level, you are in for a nice publication. The best to date possible is using microfluidic systems as microfermenters. But you still need in and outputs.

Usually you cannot keep anything alive under that condition. You generally kill, fix and stain them (not necessarily in that order).

Uh, no. It is called horizontal gene transfer.

Should be possible.

I would just go for standard textbooks. If you did not have bio there are surely some highschool books around that are good (I have no idea what books are usually used in Belgium so I cannot recommend any) and then at the same time get a decent introductory bio book at the uni level (e.g. Campbell or comparable). I would not concern myself too much with biotechnology right now as a good grasp of the basics of biology is more important as foundation. However, you may want to emphasize cell biology and molecular genetics. Actual techniques and methodology are usually taught in uni, so it is better that you focus on improving your foundation.

Developmental proteomics is still ongoing even for model organisms like Drosophila and Caenorhabditis. It is still some way off before one can try a comparative analysis of different species. Unless, of course, you are talking about individual, characterized and conserved elements of fetal development, for instance. In the sequence databases you can hunt those down individually and e.g.align them, if you want.

Interesting, but too early to know whether this will be useful. Nanomaterials are being used in drug delivery systems already and are at least under investigation e.g. for delivery of cisplatin or similar compounds into cancer cells. But whether these methods will be useful in clinical settings remains to be seen in the coming years.

Again, there is no general rule for that and there is always the question what you want to do and what kind of inhibitors you have in mind. Especially with hemoglobin many chelators (as EDTA) are suboptimal as they damage the metal core of the protein. Low temperature reduce chances of degredation, of course, but then it depends on how fast you work, what buffers you use, etc. There are dozens of different protocols out there, for some applications inhibitors are crucial, for some helpful, other useless and in worst case harmful. Basically it boils down to the question whether inhibitors will hurt downstream. If yes, you have to find an alternative way to do it. If not, adding it may or may not help.

Under strongly denaturing conditions, for example.