CharonY

Ehm, not really. It prevents agar from overboiling during the cooldown. You usually open autoclaves between 80 and 90°C, temperatures at which agar is still very liquid. They solidify roughly ~40°C.

I think you are completely on the wrong boat. See, a C60 simply consists of, well carbon. Capsids however are proteins, a far more complex composition. Check the original paper in which the crystal structure is resolved. The geometry of the phage heads is thus governed by the amino acid sequence. There are other viruses that have different architectures (e.g. retroviruses) which thus likely do not share the same common ancestors as T4 and related phages. Comparing an evolved protein structure with fullerens, even if they should share geometrical similarities is like assuming that there must be a common force between tennis balls and oranges. You are confusing very different things here.

To be honest, I do not quite get what you mean. Viral capsules usually build themselves via self-assembly. This means that the information of how to assemble themselves is already provided by the proteins which constitute these capsules themselves. The authors you cite (Fokine et al; btw it is easier if you provide links btw ) have noted that tailed phages (in particular T4 and HK97) share a similar structure in the capsule, which they share with some eukaryotic viruses. So similar structures (and also assume conserved domains) hint that dsDNA containing phages might share a common ancestor. Thus I do not understand your reasoning, as phage capsids are complex structures (as proteins go) and are not random molecules "pressed together" by some geometrical forces, as it might be interpreted from your post (at least I did). Change the amino acid sequence and you won't obtain a capsule. Judging from the link that you have given the patent is about the construction plans for a macroscopic construction unit. I fail to see the connection except for rough similarities. Like, say comparing golf balls to apples.

Actually an autoclave is not much hotter per se. The main trick is that it maintains overpressure allowing liquids to be heated up to 120° C. Essentially it is a steamcooker. Essentially you can use one to sterilize your media.

Microwaving at least in normal ovens is comparatively inefficient. Cooking agar in it for instance is not much more (if at all) more efficient than normal cooking. The heating is too heterogenous. Also, for efficient sterilization you need heating above 100° C, which only work with some overpressure. You can for instance try to moisture your dishes and then cook it for around 20 minutes. Agar will dry in that time, though. However, in all theses cases I still would only uses these to grow fast growing bacteria. It is very unlikely that they will be completely sterile.

A bit unusual. I guess that happens with high-profile fraud. But then not revoking degrees are lightly not to make a difference, as he likely won't get a (science) job anywhere now. However, this is accordance with the laws of the federal state where he got his PhD, which allows revoking the degree even if misconduct happened afterwards. In particular this law allows revoking the degree if the holder has been shown to be "unworthy" of it. "Unworthy" is meant within a scientific scope. This law is rarely invoked, though. One idea behind this is that if anyone is shown to be unworthy of the degree at any time, he/she wasn't ever allowed to get the degree in the first place. I don't know whether other (federal) states have similar rules. Though I would expect that most would rule as Glider mentioned.

Let me hint at the answer. Where does sepsis occur? Accordingly where would macrophages attack E. colis?

AFM is notoriously unsuited for soft things as biofilms, except the early phases. We have had a modified setup, but until it is published I cannot tell you more. Do you mean how AFM images looked like compared to SEMs? Well, you get toplogical information, of course. For most part a lot can be done by fluorescence microscopy. In fact, this is the usual setup to monitor biofilm formation.

The biosynthesis of dTTP requires the methylation of the uracil of one dUMP: dUMP -> dTMP -> dTTP. So based on this one can see that having dUTP is easier and less costly to synthesize than dTTP (minus one methylation). Moreover in some textbooks (a good source for this kind of trivia btw.) you can also find that uracil is less stable and eases the degradation of mRNA, which is of advantage for regulatory processes of course. Now the real question that I would ask is: why does DNA have T instead of U? The answer is equally trivial, btw.

I am afraid, I do not understand the question. Are you refer to nutrients that plants get or do you mean food of herbal origin? Also, if you are talking about translocation, are you talking about the organismic level, or are you referring to organs, or single cells?

Of course it should- I should reread my posts (or stop posting after staying awake for longer than 18h). So: Oligopeptides is used to refer to short amino acid chains, usually around or below 50. My apologies.

Mercaptoethanol is also nice. Especially if one manages to drop an unsecured 1l bottle in the stairhall... Butyric acid is a common fermentation product of a variety of anaerobic bacteria btw. Clostridia are probably amongs the best known. Anyway, try to get nitrile gloves. They smell less.

While this is off topic, I have to add a comment. The definitions of polypeptide is indeed a bit blurry. However, proteins are usually larger polypeptides which have a biological function. Polypeptides are usually used to refer to chains of amino acids of medium length (whether they have a function or are synthetic with no functions, truncated proteins, whatever). Even smaller chains are referred to as oligoproteins. As mentioned, there are no clear cut distinctions between them. However proteins are essentially polypeptides, yet not all polypeptides are proteins. On second thought I might have to add that this distinction is mainly valid in the realm of molecular biologists. I can imagine that (bio)chemists might prefer others.

That's actually what I wanted to say (albeit in a bit complicated way). I have as of yet only one instance in a phD work that had to be criticized. For masters, however, recently more and more introduction parts are copy&paste works, as these are hardly that novel (usually within the scope of the group in which it was made). Here definitions are just copied or rephrased (quite often actually losing their meaning). These parts however, are almost only read by the direct supervisor, the Prof, director, whatever hardly reads the work in detail. This might depend on the work group though (and his/her personal time). Also many of these are not that much into the work themselves (Profs tend more to be on the manager as on the science side, when the group is expanding), so they sometimes also miss factual errors.

In general STMs or AFMs (both are scanning probe microscopy techniques, not EMs, and an AFM can easily be reconfigured to a STM, just as a sidenote) reach down to the submolecular level. At least in case of hard and/or conductive molecules. In theory you can measure the tunneling interaction with a single atom with a STM and these interaction signals are then converted into information, usually height, lateral resolution tends to be worse (depends on the piezo). Now as mentioned by SkepticLance, all these techniques give you parameters of the atom/atom lattices, but there is no way to "see" anything, of course, within this size.

Maybe there are differences between countries, however in the areas of natural sciences I hardly heard of penalties in the uni (in contrast to faculties where there are usually only theoretical theses at the end). This is on part based on my personal experience (that is, the grad and undergrad students that I got), but also from colleagues (mostly in Germany but I also got a few comments while chatting with some mostly European colleagues Plagiarism is often penalized in case of theoretical work (e.g. in coursework and similar), however paradoxically not that much in the diploma/master thesis. This is apparently due to the fact that the students here are assumed to have done independent labwork (though I was told from a Prof. that it is slightly different in the UK sometimes). So essentially the thesis is setup a bit like a normal publication, albeit longer, but usually with less scientific content (obviously). So you start off with your introduction, mat&meth, results, discussion. In general, the results and discussion part gets the most scrutiny as these show what really was done. Most plagiarism is then done in the introduction and mat&meth part. As it is considered less important, copy&paste is often ignored or at most admonished (if detected at all). Those that grade also hardly read those unimportant parts. Results of course cannot be plagiarized, but the discussion sometimes has some copied in theories that simply do not fit. While this shows a lack of understanding in many unis/chairs whatever bodies responsible there is a sometimes unspoken consensus to let it slip. As in general the master/diploma thesis is often considered an too unimportant document to deny the student a further career. This I even understand. But worse, quite often the grades are not reduced accordingly and in fact penalizing those that needed time to work the stuff out themselves. But then it is always hard to grade those works, due to the different way these theses are setup. I mean, I like to let the students play, figure stuff out. Invariably they get fewer results, but the good ones get deeper understanding of their work. In contrast it is often usus to use them as mindless working drones, much like a technical assistant. In this case results roll in fast but they hardly understand what they do (good and average ones are closer together here). So, how to grade that? Also giving bad marks usually lowers the attractivity for the group. This is yet another reason to give out good marks. In general, I assume there is as of yet no real way for fairness (at least for the student’s side). The only thing I can think of to encourage those doing good work is that it is for the good of themselves, not for their grades. I do not feel very convincing, though.

The description is for (at least diploid) organims. Meaning that you got a pair of chromsomes, one from each parent. Recombination occur between them (and mechanistically between chromatids of the same chromosomesm but these are really neutral exchanges). As above already implied, this refers to the parent of the organism carrying the chromomes undergoing meioisis. Everyone carries one chromosome (consisting of two identical chromatids) from the father (paternal, not parental, btw) and from the mother.

That's easy. 1) say: "close your eyes" 2) stab eyes lightly with two fingers (avoid serious injury, unless you know how to get away with that) 3)say: "reality is everything you see right now"

Ahem, just a bit of nitpicking, but the "code" is the coupling of anticodons presented by tRNAs coupled to an amino acid. This came up much later. Now the notion of self-relplicating molecules is quite clearly the easiest to comprehend, and is the generally accepted hypothesis. As mentioned above it is also quite clear that these molecules are lilely to precede whole cells, at least what we understand as cells nowadays. How cells were assembled, however, is to my knowledge still a mystery. And whether DNA or RNA were those self-replicating molecules (they are the likeliest candidates due to their low complexity and occurence in every single organism) it is still a bit debated. Many assume that it is RNA, however others believe that RNA is too unstable alone.

Hmm on second thought I think 47 is a bit high, I have not checked it though. But in general, all organisms have a basic setup of elements. Some, however, have in addition a limited number of additional elements, not found in others. These are usually co-factors for special enzymes and by extension special enzymatic reactions (e.g. nitrogen fixation). As such of course primates have no vast differences in metabolic functions and therefore do not need these additional elements.

Or in fact, mammals for that matter... Or element wise almost all organism share the same usage of elements. There are some difference in quantities, though. But only in very unrelated or specialized species, though.

Actually I do not find anything disagreeable there. It is essentially a matter of perspective. Cells within our body are not really a perfect machine functioning in perfect harmony towards a common goal. It is really a bunch of cells all doing their thing and just happen to function together (or not in cases e.g. of autoimmune diseases or cancers). Of course this function is scripted (for a large part in genetic information, but also by other subcellular parameters). As one goes into the cell or subcellular level it becomes harder and harder to acknowledge the organism as a whole, given the many interactions between and within cells that have to work out (or not).

Wow. Well might be off-topic but apparently we biologists get a different treatment. When I tell them what I am invariably I get asked something like: " why, my back hurts for several days already, what could it be?" and if I tell them that I am no medical doctor they look at me as if I was dumb. I suppose we biologists are only allowed to appear arrogant when talking to students (or medical doctors....)

Given the breadth of the OP I would assume so. But then: Am still working as a postdoc (though hopefully not for that long anymore). Worked in universities as well as research institutes during that time. Main field is "omics" mostly of prokaryotic systems (i.e. a genomics, transcriptomics, proteomics and a little bit of metabolomics). This is about to change, a lil bit, though. I am also involved in teaching and tutoring students and phDs.

Well, if you use a plasmid in the first place using site specific mutatgenesis would be far more time efficient. The mutation has to be by chance within the gene and the vector should not be mutagenized (at least not in a negative way). For this you would have to screen all the plasmids in the hope of finding one with a mutagenized insert. Also if you want to analyze the resulting protein, you would have to express the protein heterogenously e.g. using a expression vector. If the UV mutagenizes the vector instead of the insert (which is very likely as most expression vectors are larger than a single gene) it might not work at all. Essentially it would be much faster to produce a mutagenized fragment via PCR and then clone that into a vector. You'll have to amplify the gene to clone it, anyway.