Iron and Stress

Iron is a metal that is essential for all living things as it is heavily involved in cell redox reactions and the electron transport chain (a major part of aerobic respiration). However it is strongly reactive with oxygen - outside of living organisms this leads to rust, inside it can lead to the production of dangerous reactive oxygen species - and therefore needs to be controlled and contained within the cell. In order to provide this control, all living organisms (apart from yeast, weirdly enough) use a protein called ferritin. Multiple subunits of ferritin proteins (usually 24, although occasionally only 12) form an outer shell, with a central cavity that can contain around 2000-400 individual ferric ions (iron ions) keeping them safely out of harms way.

Diagram shows the shell created by ferritin (iron, or ferrous, ions help inside). Image from wikimedia commons.

In plants, the ferritin proteins are found in non-chlorophyll containing plastids, and occasionally in mitochondria (although no one is quite sure why). Many plants contain a number of different genes coding for ferritin proteins which, due to a high similarity in sequence identity and functional redundancy (i.e. most of them do similar things) makes individual ferritins difficult to study. The small weed Arabidopsis thaliana is a good model organism in this case as it contains only four ferritins, imaginatively names AtFer1-4.

These four ferritins are expressed differently at different stages of the cell lifecycle, and in responses to different materials. The diagram below shows which genes are upregulated in response to the oxidative compound H2O2, free iron (Fe) and the plant hormone abscisic acid (ABA):

Upstream of the AtFer1 gene is a 15 base pair sequence named IDRS (iron-dependent regulatory sequence) which is used to repress the gene under iron deficient conditions. This is thought to be upregulated by a phosphatase (which would remove phosphate from a DNA binding protein bound to the IDRS) which in turn is upregulated by the plant hormone NO (nitric oxide). The kinetics of AtFer3 are very similar to AtFer1 and it is therefore thought to be regulated by a similar system. AtFer2 may be activated in a different manner, and it shows very different kinetics to the other three genes. It does contain an IDRS sequence upstream of the gene, but it is not certain whether this is functional.

Despite containing a large source of iron, ferritins are likely to function more to prevent the damage caused by reactive oxygen species (caused by reactions of free iron) rather than as an iron store. Mutant plants containing no ferritin do not have an immediately obvious phenotype (outward appearance) although if extra iron is added they have to produce a large number of energetically wasteful detoxifying enzymes, in order to combat the dangers of oxidative stress. Ferritins therefore seem to have evolved not as an iron storage system, but as a buffering mechanism, to allow increases in iron within a plant to have a beneficial, rather than damaging, effect.

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Briat JF, Ravet K, Arnaud N, Duc C, Boucherez J, Touraine B, Cellier F, & Gaymard F (2010). New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants. Annals of botany, 105 (5), 811-22 PMID: 19482877

The Predictive Power of Evolution

This post is not a breakdown of a paper, but purely an opinion piece based on my own views. I'd love to hear any different opinions people have, feel free to leave them in the comments box.

Definitions of scientific theory can vary slightly (usually depending on the theory the person currently making the definition has in mind) but they tend to boil down to a few basic elements. Explaining observational data, creating a model, falsifiability and predictive power are some of the most usual phrases used. The idea of the predictive power of a theory is an important one, both because it's a good way to make a distinction between a theory and an observation and because it imparts some kind of real-world use to the science.

One of the criticisms of the Theory of Evolution is that at first glance it appears not to contain any appreciative predictive power. You can trace the evolutionary lineage of a horse, or a whale (or a staphylococcus bacteria if you are so inclined) but you can't make any predictions about what they're going to turn into next. What strange creatures will be walking the earth in five thousand years time is occasionally brought up on random TV shows but there's hardly a way to test the accuracy, and it's not exactly science.

However this criticism seems to be conflating 'prediction' with 'predicting the future'. Very few scientific theories can predict the future. Mendelian theory can predict the likelihood of future outcomes, and I'm lead to believe that Newtonian physics can predict planet orbitals to a certain extent (provided you nudge mercury sideways occasionally) but generally the predictive power of a theory can be used to provide explanations for observations without needing to try and head into the future at all.

To use an example from my current revision: chloroplast gene movement. Chloroplasts are little organelles in plants that carry out photosynthesis and contain the green-coloured pigment that makes plants look mostly green. They are thought to have arisen (and there is by now lots of substantive evidence for this) when a free-living cell engulfed a little photosynthesising bacteria (image below taken from George Washington University page explaining eukaryote evolution):

As the little photosynthesising bacteria contained its own DNA the new chloroplast containing cell now has two genomes, the one in the nucleus and the one in the newly-made chloroplast (ignoring mitochondria for the minute to make things simpler). However when you look at modern plants and compare the chloroplast genome to any bacteria genome you can see that the chloroplast genome is massively reduced. Most of the genes have been lost. Further research will identify several of these chloroplast genes inside the nucleus. The genes have migrated out of the chloroplast, and into the nucleus, where they are being expressed by the nucleus.

There's plenty of reasons why the genes would want to be in the nucleus. It provides centralised control, it keeps the DNA safe from all the reactive oxygen species in the chloroplast, and it means that the chloroplast genes can experience sexual selection. However not all of the genes have left. Some have remained inside the chloroplast, and the question is, why? If the nucleus is such a good place to be, why do some genes get left behind?

In answering this (in fact in answering many question here, including why the genes left as well as why some remain) the theory of evolution can be used to provide a predictive framework in which to suggest an answer. These predictions can then be tested with the data to see which ones fit. In the case of why genes remain in the chloroplast, for example, our theory tells us that if there is a reason (they might just have remained through chance if it was one event that transferred the genes, or they might still be moving) it will be to give the cell an evolutionary advantage. These are genes, and there is a lot of selective pressure on what happens to genes, especially in bacteria, which have a limited supply. The genes that stay behind must provide a selective advantage, there must be a reason why these genes help the chloroplast, and the cell to survive, better than they would if the genes moved to the nucleus.

Once in the nucleus, the genes are used to make the corresponding protein, and this protein is then transported back into the chloroplast. In view of this, one of the first suggestions made was that the genes left behind coded for big bulky proteins that were hard to transport through the chloroplast membrane. Chloroplasts that lost these genes would loose valuable proteins, leaving them at a disadvantage. It's a nice prediction, but unfortunately it got shot down after a close examination of the genes that had actually moved revealed that some of them did code for quite big bulky proteins. And artificially moving some of the bigger and bulkier protein-coding genes into the nucleus showed they could get back into the chloroplasts quite happily, although not quite as efficiently.

Another prediction made (which is looking far more likely) is that the genes left behind very specifically control the redox potential (the balance of positive and negative ions) inside the chloroplast. Due to the photosynthesis the chloroplast is carrying out, the redox potential can change quite dramatically (and regularly) and it needs to be sorted out quickly if it does, as it has the potential to cause a lot of problems within the chloroplast. Having the genes that need to respond to redox change in the nucleus means that a) it takes a lot longer for the signal to get to the nucleus and get the proteins made and b) once the proteins are made they will be sent to all the chloroplasts, despite the face that different chloroplasts will be in different redox states. So far the evidence supports this prediction.

Without the theory of evolution behind this, there's almost no reason to look for a reason. Why the genes moved, and why some stayed behind can be answered by 'they just did'. The framework of an answer that requires an increase in the 'fitness' of the resulting organism helps to give suggestions, and predictions, that can be looked into with further study and gives a focus for directed research.

Extended Hiatus

I had hoped that my little holiday-hiatus wouldn't last much longer than two weeks. However due to a certain volcano going off, I am now stranded in the land of Dial-Up Internet and not quite sure when I'll be getting back. The time I do spend on the internet is spent contacting my partner, trying to download papers and trying desperately to get in touch with my supervisor who has an electronic copy of my (as yet unchecked) dissertation I would really like her to take a look at.

I have a horrible feeling she's stuck in an airport in Canada...

So while the forces of plate-techtonics conspire against my Finals I don't have all that much time for blogging. I'll return as soon as I can, with lots of science stuff (most of it about plants probably, as I'll still be revising) but until the ash clears there won't be anything.

It's really irritating, as I want to get into proper paper-trail revision, which I can't do without an internet source. And the deadline for my dissertation is the Wednesday after next, so I really need to be back by then.

Also I have a library book with me that just went overdue...

(On an unrelated note something happened on the 11th - my page views took a spike. Thank you to whoever-it-was that caused that! Much appreciated, expecially as I'm not able to write much at the moment).

How The Animal Lost Its Sensor

Two-Component Systems are one of the major sensory systems used by bacteria to detect and respond to changes in both their outside environment, and their internal state. I cover them in more detail here, but just in summary they consist of two proteins,a sensor and a responder. The sensor senses the change, and activates the responder, which binds to the bacterial DNA and leads the production of a protein that will enact a suitable response.

Although Two-Component Systems (TCS) are found in all three superkingdoms of life (Archaea, Bacteria and Eukaryotes) they are suspiciously absent from the animal kingdom. Plants have them, as do fungi and several protazoa, but they just aren't present in animals. For this reason they've been looked into as potential antibiotic targets as knocking out the Two-Component Systems of most bacteria is fatal.

Why don't animals use TCSs? To answer this you have to start looking at the evolution of the system itself, because despite being nominally present in eukaryotes such as plants and fungi, TCSs are used very differently in bacteria and archaea. Bacteria use TCSs for sensing a wide variety of signals; stress, metabolism, nutrient regulation, chemotaxis, pathogen-host interactions etc. in eukaryotes on the other hand, they are used sparingly, for ethylene responses and photosensitivity in plants and osmoregulation in fungi and slime moulds.

Bacteria (especially soil bacteria which have a lot of environment to sense) can contain up to 50 TCSs although many internal parasite bacteria (with a lot less to sense) contain far less. The maximum for Archaea is around 20 TCSs. Eukaryote number drop right down, with only one in the yeast Saccharomyces cerevisiae (one sensor kinase and three response regulators). None have yet been found in any animal genomes, or in the few partial protist genomes sequences (although I doubt if anyone's had a complete scan through the protist genomes for them).

Comparing the TCSs of Bacteria, Archaea and Eukaryotes leads to the interesting conclusion that the bacterial and eukaryotic systems are far more closely related than the archaeal, and in fact are thought to be monophyletic (all evolved from a single common ancestor). In contrast, the archaeal TCSs appear to be polyphyletic and some archaea lack TCSs entirely. It's therefore thought that TCSs originated in bacteria and spread by horizontal gene transfer to both archaea and eukaryotes (until the eukaryotes developed a nuclear membrane). In eukaryotes very little further diversification took place, whereas the bacterial TCSs diversified widely, and occasionally passed new systems back to the archaea. I've tried to show this in the diagram below:

Diagram made by Lab Rat. Red arrows show the movement (straight arrows) and duplication (curved arrows) of TCS genes. No horizontal gene transfer can take place in eukaryotes after the nuclear membrane (well....it *can* do but very, very rare) although gene duplication may still have occurred.

The eukaryotic kingdom appears not to have contained very many of these TCS genes to start with, and the animal kingdom may just have lost the very few it possessed. This makes sense from the point of view of cellular control because while TCSs are very useful in the small genomed and non-nuclear membrane containing bacteria, it's less clear how useful they are in eukaryotes as a whole. Introducing a membrane around the nucleus makes it harder for proteins to get in and bind to the DNA, and introducing systems of membranes inside a far bigger cell makes it harder for a simple two-component system to sense what's going on. Added to which, cells inside a multicellular organism don't really need to sense what's going on, they get told what's going on by the surrounding cells and circulating hormones.

Whatever the reason though (and any other ideas would be welcomed, the above paragraph is mostly speculation) it is clear that despite this system being vital for bacteria it isn't used widely, or most likely at all, in animals. Research into this would be particularly useful against opportunistic pathogens which tend to have a large selection of two-component systems to allow them to adapt to different lifestyles depending on the conditions of their immediate environment.

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Kristin K. Koretke , Andrei N. Lupas , Patrick V. Warren , Martin Rosenberg , and James R. Brown (2000). Evolution of Two-Component Signal Transduction Mol Biol Evol, 17, 1956-1970

Wolanin PM, Thomason PA, & Stock JB (2002). Histidine protein kinases: key signal transducers outside the animal kingdom. Genome biology, 3 (10) PMID: 12372152

The Impact of Impact!

I went down to London for the weekend to see an exhibition by the Royal College of Art entitled "Impact!" which was a colaboration between designers and research teams to explore the potential impacts and implications of future scientific research. I always like watching when the worlds of art and science collide, and it was a good excuse to get away from my dissertation for a while.

I've done some work with designers before (during my last summer project, I wrote about it here) and I loved it. Designers bring new ways of looking at a project; they have the ability to take science out of the lab and into the real world, while still addressing social and ethical concerns. What I saw at Impact! was the ultimate in science communication and to be honest I think it showed the reasons most people get into science in the first place. It was fun, slightly geeky (five dimensional cameras!) colourful, thought-provoking and all with a wonderful overtone of sci-fi.

The project I enjoyed most (probably because I've met the designer, and saw little sneak-peaks of of it being constructed) was "Cellularity" by James King. This explored the potential of using cell-like structures to deliver pharmaceutical products into a patient, structures that over time, and years of research became so cell-like that they begin to blur the devide between life and non-life, bringing up fundamental questions abut what life even is.

Cellularity from James King on Vimeo.

Start by considering an empty cell filled with drugs and swallowed, like a tablet. Inside the body the membrane dissolves and and drug is released, similar to chemical pills. Clearly the 'cell' (if it can even be called that) is dead. Move on, design a cell which can both produce the drug itself (from a small DNA coil inside it) and replicate itself. Is that alive - or is it merely a biological drug-dispenser?

Next stage...suggested for patients who respond to no current therapy, allow the little drug-making cells to breed within the pateint, replicating in a semi-asexual manner, so that each offspring is producing a different drug. While James indroduces 'death' as a later stage in the line denoting life from non-life I think that for pure health and safety reasons it should probably slot in here. Cells that produce drugs that could potentially harm the patient must be able to die, either by self-destruction or (as James suggests) signalling to the bodys immune system to come and take them away.

If you start giving these cells the power to sense their surroundings as well (maybe to predict the best drug to produce) you get very close to something that can be called life. It's artificial life, life designed exclusively to serve the humans that use it, but life non-the-less. At this stage, it becomes almost meaningless to talk about 'life' and 'non-life' as separate boxes, and instead they become a gradiant, a sliding scale between the living and the dead. This is something that is starting to be appreciated even now when considering things like virus's, or prions. A prion is an infectious protein element, with no DNA or cell wall yet it is capible of replicating and evolving (and consequently sticking two fingers up to Dawkins a bit). If a small piece of twisted protein has a passing claim to 'life' the definition of what life actually is starts to become somewhat hazy. And scientists have made virus's in the lab, creating what could potentially be classified as living organisms from 'dead' pieces of DNA and protein.

One thing that worries me though, how many scientists went to Impact!? I'm sure plenty of designers did, and I'm sure they got a lot out of it, I certainly did. But this is really something I think more scientists should get engaged with. Designers are fun to work with, and they're good at communication especially to a general audience. They make colourful posters, and five-dimentional photography machines, and wierd spiky machines that hang from the ceiling. They bring the excitment back into biology, they remind you why you went there in the first place.

Also I really, really want a five-dimensional camera...

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Where my bio began...

Sigma is doing a promotion/competition thing at the moment called "Where bio begins" which seems quite interesting. The aim is to get scientists to show, through a variety of media, what sparked their interest in biology, why they decided to study it and why they find it so fascinating. I'm not sure whether I'll enter for the competition (they need my real name unfortunately) but it's a great idea and it sort of got stuck in my head. Why am I doing biology, and where did bio begin for me?

There are a lot of answers to that. Something about my childhood probably, about how I found everything exciting and was encouraged to explore a lot. Something about my schooling, which was quite science oriented. Something about my personality and the traits which allow me to love lab-work, even when it hates me in return, and probably something about science itself, which is so amazing and beautiful.

I think the biggest moment for me though was when I first saw a picture of the inside of a cell, containing all the details of the organelles. I was sixteen at the time, and cells up until then had just been drawn as blobs, with maybe a little blob inside labelled 'nucleus'. To suddenly see the whole crowded, busy and breathtakingly complex cellular interior was a bit of a revelation because basically what my mind saw was something like this:
It was another world in there. And I've been hooked on that world ever since.

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Map is (c) Me. It was fun to draw and I am very proud of the trees and the boat. My favourite bit is the dragon sitting on top of the cell, because it's a dragon sitting on top of a cell.

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Reflections on Lab Work

I've just come to the end of my project for this year. Last week was the usual flurry of tidying, organising the freezer, and making sure all my stuff is on the Lab Computer so that anyone else who wants it can use it. I tried very hard to feel some sort of nostalgia about leaving, but to be honest all I managed was a sense of supreme exhaustion and slight relief. Besides, I'll probably be nipping in an out of there to collect results pictures, protocols, etc. for my write-up.

So I thought I'd just do a quick run-through, for anyone who's interested, about my lab experiences. I've done four lab projects to date, and enjoyed every one of them. I can't even say which one I enjoyed the most, they're all special in different ways.

1) My First Project Ever was working on bacteriophages (viruses that infect bacteria). It was fairly heavily supervised, I was working with a PhD student and helping her on her project. It was probably the most fun I've ever had in a lab; there was no pressure for a big write-up (just a small report for the funding body) or excessive pressure for me to get results, and I felt very useful being able to help. It was also the first time I'd been paid for lab work, and got that amazing rush of "woah....people will give me actual money for this!"

I started this blog during that project. The entries from back then make me laugh now. :)

2) Second project was for my course, where I switched to working on Streptomyces. Again, I was working quite closely with a PhD student, but she had kids and used to have to leave the lab about midday to take care of them. By the time the first week was up we'd worked out a system; in the morning we'd go over all the work I needed to get done, and in the afternoon she'd leave and I'd get on with it. It was quite a nice step up, as I was still being supervised, but I was doing the work all by myself.

The blog kind of died in that period, because it was insanely busy and I hadn't found out about research blogging yet.

3) The third project was the synthetic biology one, which wins the award for Most Stressful Project so far. As it was meant to be student-based we (there were seven of us, only four of whom were biological scientists) were pretty much dumped in the lab and left to get on with it. We had meetings with the supervisors once a week, and we had a PhD student to help us out (for which we were incredibly grateful) but other than that it was all down to us.

Considering I was the only one in the lab who'd ever done a project before it's amazing we managed anything really! I've got a lot of blog posts from that time, mostly because I spent about four weeks in the middle of it failing to make two point mutations. This involved lots of waiting around for gels to run, PCRs to happen, and ligations to fail, during which I would happily type away at my computer. Also at some point around then I discovered researchblogging.org and completely took off with the research side of things.

4) The project I'm currently writing up. This one has been the first project I've really thought of as my own (which makes the lack of conclusive results a bit harder to take). The lab is quite small, and as the PI and post-doc were quite busy last term, I was organising experiments and procedures pretty much on my own. I'm looking forward to the write-up, especially now I've drafted it and discovered that I actually do enough to write up. I feel more personally attached to this project than any one I've ever done before. The knowledge that my little samples are going to be sitting in the freezer for a long while before anyone bothers to dig them out actually does hurt a little. The next three weeks of write-up are going to be fun though :)

I'm quite surprised and proud that I've managed to keep up regular blogging throughout the course of the project.

5) I've already organised a summer project! As usual, there will probably be only the vaguest details of what I'm actually doing on the blog, especially as this project really should lead to a paper. But stay tuned for more bacteria-related posts. I'm sort of hooked on blogging now, and it'll probably take a lot to get me to stop.

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Norovirus and Clinical Research

I've written a lot about bacteria and plants over the last few weeks, so in celebration of the fact that my project is finally on it's way out (with a whimper rather than a bang, unfortunately, but that's how it goes sometimes) I've decided to descend into the world of viruses. I've also decided to have a go at deconstructing some clinical papers, to make a change from academia. The difference between clinical and academic research can probably be described as follows (and I'm pretty sure I've stolen this quote from somewhere else, but can't remember where):

Clinical Researcher: "That's interesting, but it is useful?"

Academic Researcher: "That's useful, but is it interesting?"

[Industrial worker: "That's useful and interesting....can we sell it?"]

Clinical papers therefore have a different slant from academic ones. They tend to be a lot more precise, a lot clearer. Most will include data from actual people rather than just biochemical data, and the real-world applications come across as the main focus of the study, rather than just tacked onto the end for funding purposes. It comes across in presentations as well, I went to the Society for General Microbiology conference last year and you could usually tell within about ten minutes whether you were listening to an academic, industrial or clinical researcher.

But anyway...on to the papers, which deal with Norovirus, a viral infection usually thought of as a mild (if unpleasant) winter vomiting disease. Norovirus is an RNA virus, which means that it consists of a coil of RNA wrapped up inside a spherical protein coat, as shown to the right

(image taken from the Naked Scientists):

The virus enters the body through the mouth, and invades the small intestine, resulting in lesions in the small intestine tissue and an increase in mucus production. This affects the absorption of nutrients, and leads to build-up of food in the stomach (which can't move down into the intestine) which in turn leads to vomiting and diarrhoea and generally feeling unwell.

Norovirus usually peaks during the winter months, probably because during the winter people tend to spend a lot of time stuck in the enclosed areas with other people. However in 2002, this decline during the summer months halted, and incidents of the disease began to increase, particularly in the over-65 age range. This is due to the emergence of a new variant of the virus which has a higher human-to-human transmission and is therefore more likely to spread in areas where people are living in very close proximity, such as nursing homes and hospitals.

As these places tend to be full of people who are not at their most healthy, this can lead to serious complications in the disease. The damage to the intestines can lead to dehydration which in some cases has been severe enough to lead to kidney failure. Diarrhoea and vomiting cause potassium loss, which can lead to problems in the heart. Deaths are thankfully uncommon, but have been reported.

What this means is that norovirus shouldn't really just be thought of a mild disease any more particularly (which one of the main issues with for clinical researchers) when it happens in hospitals. There's no vaccine against it, as multiple strains exists and having norovirus doesn't really give you much of a defence against getting it again. There has been some work done with the capsid proteins (which surround with RNA of the virus) but as yet this is still happening in mice, and I'm not sure whether it's even entered clinical trials. The best current defence against norovirus is still just to keep things as clean as possible, especially in places where many people are in close proximity, to keep very ill patients away from as many other patients as possible, and to tell doctors to stay at home if they wake up vomiting.

One of the great things about Medical science of course, is that it's an ongoing process and we are the data-sets. This summer rolling around (soon, hopefully!) will bring more information about the state of norovirus, whether the trend in increasing virulence is still around, or whether it's starting to die down. Either way it's a good reminder that sometimes all it takes is a particularly busy hospital and a blip in a piece of floating DNA to turn a relatively harmless disease into a much more problematic one.

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Hane Htut Maung (2008). Norovirus Infection: An Underestimated Danger Cambridge Medicine, 22, 22-24

Lopman BA, Reacher M, Gallimore C, Adak GK, Gray JJ, & Brown DW (2003). A summertime peak of "winter vomiting disease": surveillance of noroviruses in England and Wales, 1995 to 2002. BMC public health, 3 PMID: 12659651

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International Women's Day

"What does “equal rights for all” mean to you?"

It means being able to look at any other person in the world and being able to think: Yes...I would be not be significantly more unhappy if I had been born you. I would not be any more ashamed, I would not be any more afraid, I would not be any more unable to be happy. I might have a different lifestyle, different thoughts, different feelings, maybe even a different set of values than I do now, but I would be no less able to enjoy my life.

It means watching what I say, examining what I think, trying to see inside my head from other peoples point of view. If I were you, would I laugh at that joke? If you were me, would you say it? It means making myself listen to other people, listening for clues as to how they see their world, why they act how they do, making myself imagine thinking like that, acting like that.

It means accepting that just because two views are different, doesn't mean that one of them is 'Right' and the other 'Wrong'. Finding more dimensions to see the world in, more colours to paint thoughts with, more ways of being. Not to laugh when someone does something I find odd, but to watch, to understand, and to accept. To be able to feel differently to you, in the knowledge that neither of us considers our point of view superior, just different.

It means being able to look at You, and seing someone that could be Me.

Other participating blogs can be found here.

Redecorating

I'm trying to personalise my blog a little more, so that it doesn't look the same as all the other blogs written by people who like olde-style parchment. I made a bit of a change a few months ago, when I expanded the size of the actual writing area, but unfortunately it left me with a weird dark line down the right hand side of the page that I would love to get rid of.

I got the new background from squidfingers which has a lot of really great tilling patterns in case anyone else was thinking of doing some blog redecorating. It's pretty similar to the old one, but let me know if the repeating little white lines make anyone's eyes go funny!

So there might be some changes over the rest of the week. I'm really looking for a new parchment-style background that I can fit under my words (without the dark line - I got that by just repeating my current template sideways), preferably with some kind of ornamental line under the "Lab Rat" title. I'm also considering a wholesale move to black and white. It might be cleaner, but I think I would miss the gentleness of the browns. Besides, my partner once told me that if I was a colour I would be brown. (I'm still trying to work out if that's a complement - I've always seen myself more as yellow, which I guess isn't that different...).

What I think would be great is a little picture in the top right hand corner (opposite the "Lab Rat" title) but I have no idea how to do that, and I don't quite have a suitable picture. I'm tempted to push a little more of the money I don't have towards Alice, to get an awesome spiky-haired rat in a lab coat. Maybe once I get a job.

Anyway. There probably won't be another science post this week, because I've only technically got one week of my project left *FLAILPANIC*. Times like this you really wish the ligations had worked.

If you miss the science, head over to researchblogging.org. We've had a sudden rush of new people joining due to the Awards getting publicised!