CharonY

I do not know what you mean to liquid composition, and no, they do not turn into dust. Dust is comprised of extremely large particles, much larger than any single protein. Instead, proteins get degraded over time. Tertiary structure (and hence function) can get lost very fast, further degradation depend a lot on the environment. The quickest degradation is generally due to protease functions.

Can we have giant mutated hamsters involved, too? Please?

Depends a lot on the the protein and the environment. Some are inherently more stable than others, but degradation due to external factors weigh in heavily. Relevant parameters include the liquid composition it is in, temperature, presence of other enzymes etc. It also depends a bit on what you mean by lose their structure. The tertiary structure is for the most part relatively unstable, at RT and without specific buffers most will readily lose their active confirmation (again, with some exceptions). But the proteins are still present and may be detectable (if inactive).

To be fair, the type of experiments you suggested have a very narrow scientific value. But the suggested book delivers protocols and is imo one of the best rounded books you could get to get an overview of current and basic methods in the area of molecular biology. For textbooks more towards the non-experimental side, the Alberts is quite good (Molecular biology of the cell). For Biochemistry the Stryer pops to my mind. There are many more but these are the titles that I still remember.

It should be noted that life is not an easily measurable property and as such precise definitions are going to be iffy. Especially as the definitions are exclusively based on what we found on earth so far. I would take it more as a guideline rather than a strict definition. But then this is true for much of biology in general. Squishiy things do strange things, as I like to say.

It is really blurry indeed. What I would recommend you is pick up a copy of Sambrook, Molecular cloning. it is a method-based book that also describes the processes involved quite well. There may also be more basic textbooks which would benefit you. At this point a good textbook is really your best friend.

From what I have heard analyst with a PhD are less common. Job prospects are tricky, especially now. With no job experience it is best to get your foot into the door somehow. One thing is obviously to search for open positions, but that alone tends to have a relatively low success rate. Ideally collect some names of people in the companies you want to work for. Job fairs are an easy way to get face time (and collect contacts). Alternatively ask around if someone you knows someone in the biz that you could talk to. In any case, try to get a (non-dead-end) entry level fast, with even a little bit of private sector experience you can increase you market value quite dramatically.

The problem I see is that high level assumptions are trying to be discussed but with no foundation on which to discuss it on. As others mentioned, learning that will take longer than a few lines in a forum and as such all discussions will be superficial and inaccurate at best. Also a true specialist in this area may be able to come up with some nice analogies that will satisfy the layman (without providing specific answers, though). But I freely admit that this is outside my range of expertise. That being said, perceptions or emotions are not the result of single or even few pathways, there is strong interconnection between certain neuronal activities but is also affected from feedback from the rest of the body. The area where these sensations finally arise are located in the brain, but even that is not quite as trivial. For instance, the amygdala is associated with the perception of emotions, including fear. In people with Urbach-Wiethe disease the amygdala is dysfunctional and as a result they show e.g. only minimal levels of fear upon stimulation. However, in these people an increase in CO2 levels still induces fear of suffocation, indicating that there are other pathways upon which the body senses and translates this sensations into a feeling. (see Feinstein et al. 2013 in Nature Neuroscience). One can speculate how things work without further reading up on the basics, but frankly, it is a bit like trying to do calculus using your fingers.

The high viscosity of the solution is not due to precipitation of SDS but due to the glycerol. Even if SDS precipitates, the solution would still be liquid (with SDS flakes floating around). Generally I would also avoid heating and at that concentration also unnecessary. Did you dissolve SDS only in buffer (i.e. without glycerol)? Alternatively you could reduce the SDS concentration a bit (common values are somewhere between 6-10%) as well as glycerol (down to 40%). Third possibility is to create less strongly concentrated loading dye, but if working with dilute protein samples that may not be ideal (though 5x concentrated is still very close and you are not as close to the solubility limit of SDS). Also, if you freeze your buffer, do not forget to let it get to RT before pipetting. For the most part I do not recall specific issues with creating 6x loading buffers, but for various reasons I started using 5x for most standard applications.

Due to the lack of knowledge of the basics, a satisfactory answer simply cannot be given. At least not without teaching a whole course on cell biology and some neurobiology. Essentially you can imagine that the chemicals are transported to various parts of your body, including your brain, get recognized by affected cells via specific proteins on their surface (read up on "receptor binding") that leads to um.. complex stuff within the cell (due to "signaling cascades"). The overall result is a physiological reaction that can be perceived as a certain type of feeling. The way the physiological change or response actually gets translated into a perception (i.e. feeling) is quite complex and poorly understood.

Fire, on the other hand could be considered a replicator of sorts. Neither example has anything to do with biology so I am not sure how that fits into this section?

There may be something lost in translation, but "testing the DNA binding domain of a protein to a transcription factor" does not really make sense as a transcription factor is generally a protein with DNA binding properties. Thus it would imply a protein-protein interaction. It would help if you clarified what is supposed to bind to what. I will for now assume that you want to test the binding of a protein (or its DNA binding domain) to a cognate DNA region (essentially an EMSA or electrophoretic mobility shift assay). Assuming that to be true I have some issues understanding the image. What is in lane 1? It is labelled as no protein, but what is there? Are the fragments in 2-4 referring to specific fragments of the DNA-binding protein? Or does it refer to a DNA-fragment? On the same note, what precisely is in lane 6-8? Are the fragments referring to DNA now, or to protein fragments? If the fragment are all referring to proteins, where is DNA added? Also what kind of visualization is shown in the gel? I.e. are only the proteins dyed or are DNA and protein visualized? I could start guessing and assuming that the fragments are really referring to DNA stretches, but I would prefer if you could clarify. Note that domain refer to specific regions on a protein and not on DNA..

The problem with this kind of arguments is that it is based on a complete lack of understanding of genetics and argues from there. One cannot really deconstruct individual arguments without pointing out that everything is nonsense and educated from the very basics, which would take more time than most (on either side of the argument) are willing to invest. Nonetheless, a few points to address: - changes in genome size can be quick and dramatic. Common mechanisms are duplications of whole areas and even chromsomes, but also due to mobile genetic elements such as viruses, transposons, plasmids, integrons and so on. These changes may not persist through the generation if they are deleterious, but there are plenty of examples in which they do (just think about polyploidy, i.e. multiplications of chromosomal sets) in plants. The additional genetic material may not even change the phenotype, but they allow for mutations and creations of genetic variants which may not have beem possible with a more restricted genome. This leads me to the topic of mutations. Of course mutations do create novel material. A change in a base can result in a change in an amino acid, which in turn may change the function of a protein. More dramatic changes can be induced by changing the expression pattern (e.g. by mutating regulators or regulatory DNA sequences). There are plenty of examples for that too (again, basic genetics). The summary is basically that evolution has nothing to do with randomly adding base pairs to the mix, nor do the molecular mechanisms work that way, which makes all the toying with numbers (I am hesitant to even call that math) rather pointless.

In case someone is wondering, OP is referring to two ecotypes of Arabidopsis thaliana (Columbia and Landsberg erecta). Both have been sequenced, so you should find the at the respective data repositories from the original sequencing consortia or on the NCBI server. Which one you need depends on whether you want AA or DNA sequences (title refers to gene, post implies protein)...

The amino acid distrubution can vary quite a bit if we look at all organisms (at most one order of magnitude, usually far less). The largest differences are found with extremophiles which require specific adaptions to allow their proteins to function under extreme conditions.

Also chances are that this will be the time where you will have most fun with science (long enough to appreciate some of the finer elements of science, not long enough to be bogged down by other duties). Have fun, but also try to get to know people and stay in touch. You never know what contacts can be good for.

OK, this pretty much all wrong. The major discussed actions of silver particles involve the formation of oxidative stress and inhibitaiton of enzymes due to interaction with thiol groups.

Generally the silver ions are what kill off bacteria, thus the form of silver is relevant. Nanoparticles are, due to their larger surface, more effective, for instance.

Well, I assume they refer to obsessive praying, or the inability not to pray.

The funnel is an elegant way to do it. Parafilm is a really bad idea. If you do not have access to anything, I would take bottle that is sealed tightly before shaking or vortexing phenol. For the most part, a stirring bar works also well, but I would disrupt the strring a little bit every now and then and restart, to ensure homogenous mixing. In the end it should look like a nice emulsion, without any obvious separation. The problem with decanting is that either you will waste quite a bit (if you want to avoid getting the aqueous phase) or you will have to pipette the last bit rather carefully. Certainly not ideal, but doable.

For a career the choice of course will mostly have little to no impact (especially if you do not precisely the job you wan to get into). In addition the actual topics covered under these names are going to vary quite a lot from university to university. IMO the most useful courses are heavy on the analytic side (as they are more universally applicable), but this could be covered by all of these topics. What you learn (and thus, how useful it will be to you) will be much more dependent on the design of the course and the abilities of the teachers, rather than the overall topic.

Education and use of condoms have reduced spread of HIV. From the 80s to the 90s there was a steady decline in new incidences and has more or less remained steady since then (for most of Europe and the US at least). In addition scientific and medical advances helped in the diagnosis and treatment and management (though not cure) of the disease. It is not a novel finding that some youngsters (and others) miscalculate or ignore risks. That is why education can help.

Complacency is unfortunately very common (I am certainly also guilty of it at times). I do have the advantage of having a mix of hazardous and non-hazardous cells (e.g. prokaryotes) and I try to slip into different mindsets for each type of work. Regarding growth in the eyes, I would not think it very likely considering that most cell lines are wimps and require quite some pampering (though you will know more about your particular cell line than I do). Also there would be issues in adherence, considering that there are quite a few mechanisms to get rid of stuff from our eyes. But a check every now and then is certainly not the worst one could do.

I assume you meant the bottom right is interphase and the middle is prophase? Look at the nucleus, do you see any differences?

This can refer to a lot of different things and hence, techniques. Structure can be elucidated by e.g.: -crystallography -NMR -MS -molecular biological techniques Functional analyses often include: -mutagenesis/ knock down -fluorescence based investigations -in vitro analyses and many more (as well as combinations thereof). It really depends on the questions the lab is trying to answer.