Thanks for this post, Matthias. I was not aware that so many of the other programs were backed by publishers. (I use Jabref, so I'm in the clear.)
I also think this article is oddly-timed to write about Mendeley without mentioning the uproar over the recent buy-out by Elsevier. I think you've touched on good points with this comment. As a scientist, open-source is extremely important, not only for ideology, but also full-disclosure of what the program does.
To expand on Kurt's point about "no guarantee for long term usage", an example is Elsevier's recent purchase of Mendeley. Some critics suggest that Elsevier might shut down Mendeley, and I've read others suggest they Elsevier might introduce anti-competitive philosophies into the product. Hopefully this will be addressed in the next article, though!
I agree. The title of this article is misleading, as it's really about using NCBI BLAST, not BLAST per se. BLAST is so much larger and more powerful than just what NCBI's web interface allows! Similarly, my organism isn't in NCBI, so it's irrelevant. Another good option for checking primer specificity is ipcress.
Have you ever tried Jabref? It seems to share all the features of Mendeley, and seems very powerful. Unlike Mendeley, it's open source, which is nice. I use it with LyX, and it integrates well. The Jabref devs are very open to feedback as well.
Well, in the absence of a reply, I've researched this some more... From your first reference link, "increasing the OH- concentration of an aqueous solution has the effect of decreasing the H+ concentration, because the product of these two concentrations must remain constant", which contradicts your paragraph.
"If you were to add more H+ to this solution, more H2O would dissociate to generate a matching amount of OH-. The more H+ you add, the more dissociation of water occurs, moving the equation to the right."
Is this correct? AFAIK it works that other way around. If you add more H+, it would drive your equation to the LEFT. K_w, the ionization constant of water, must stay constant. K_w = [H+][OH-] = 10^-14. Hence, if you add [H+], [OH-] must decrease, creating more H2O.
If your primary concern is consistency, then working *quickly* is inconsistent with that aim. This would amplify the difference between samples, as proportional (linear or logarithmic) time has a greater effect when the numbers are small. The difference in protease activity between 1 and 2 minutes is much different than 20 and 21 minutes.
I'm used to a bias toward Homo sapiens in science reporting generally, but this is ridiculous! What about all the other "cells" that scientists culture? Parasites, algae, amoebae, etc., etc. I'm sure most varieties of "cells" do NOT want 37°C, nor 5% carbon dioxide. I don't mind if most articles are directed toward human-orientated scientists, but don't assume that encompasses everyone!
For scientists particularly, I think TeX is a much more versatile and powerful word processor (also free/open source). It's a fairly steep learning curve, but ticks all the boxes. If you use a frontend such as LyX, it's very easy to learn. On the Mac, LyX syncs excellently with a fabulous reference utility called BibDesk, which is worth a look even if you don't use LyX/TeX. Better than Papers, and free!
My understanding is that if smaller proteins are running through the membrane, then you need to transfer at a lower voltage, not for less time (assuming the time is correct for the larger molecules). The theory is that lower voltage will not allow the transferring proteins from becoming "unstuck" from the front face of the membrane.
Also, most commercial sample buffers include Coomassie G250, which tracks the ion front when running the SDS-PAGE gel. Hence, you can just stop the electrophoresis run when the dye front reaches the bottom of the gel.
I've not heard of having to fill empty lanes with loading buffer. What is the theory behind this? I did sometimes get smiling even when all lanes are loaded, but changed to pre-casts, which seemed to fix it.
I also think this article is oddly-timed to write about Mendeley without mentioning the uproar over the recent buy-out by Elsevier. I think you've touched on good points with this comment. As a scientist, open-source is extremely important, not only for ideology, but also full-disclosure of what the program does.
Jabref is excellent, and is also free (as in freedom, as well as "doesn't cost anything") and integrates excellently with LyX.
Bibdesk is/was also excellent if you are using OS X.
Is this correct? AFAIK it works that other way around. If you add more H+, it would drive your equation to the LEFT. K_w, the ionization constant of water, must stay constant. K_w = [H+][OH-] = 10^-14. Hence, if you add [H+], [OH-] must decrease, creating more H2O.
Cheers.
Also, most commercial sample buffers include Coomassie G250, which tracks the ion front when running the SDS-PAGE gel. Hence, you can just stop the electrophoresis run when the dye front reaches the bottom of the gel.