As the conference winds down, I think it was, all in all, a good thing. It will be interesting to see how it develops. Will it become a mega-meeting, like the ACS meetings, or will it find some sort of niche, disciplinary or otherwise?

It was quite windy for most of the week, with the main plenary tent creaking and popping like a schooner in full sail. I thought about making some corny pun about these being the winds of change sweeping over Europe, as they find their collective identity and become a force to reckon with. This would have been just too pat though, and in any case, we will have to wait and see.

And so, Viszontlátásra from Budapest!

Posted by Emma Marris at 07:11 AM | Permalink | Comments (0) | TrackBacks (0)

A big conference just isn't a big conference without a lot of handing out of medals. So here's congrats to Jonathan Nitschke of the University of Geneva, for winning the European Young Chemist's award. He got an IOU from the Italian Chemical Society for 1,800 €, and a nice gold medal. Lee Cronin promised me that if he didn't win, he would get up and shout 'It's rigged! It's rigged!', but unfortunately, he got one of the silver medals, and so we didn't get to see a temper tantrum in the tent.

Posted by Emma Marris at 07:10 AM | Permalink | Comments (1) | TrackBacks (0)

Analytical chemists won't run out of work any time soon. The world is reassuringly full of unknowns. Perhaps less reassuring is the nature of some of these unknowns. Koni Grob at the Kantonales Laboratory in Zurich, which he calls 'a nano FDA', has been looking at the compounds that food packages shed into the food we eat. His most recent focus has been on the plastic gaskets found inside jar lids. He finds that when oil–like that in tomato sauce, for example-touches these gaskets, all sorts of known and unknown things leach out into the food.

'Many people want to have bio or organic food, but I think that they are not aware that by far the highest source of contamination is food packaging.' Many compounds, like epoxidized soybean oil and Bisphenol-A diglycidyl ether are present in oily jarred foods in levels far exceeding the maximums for contamination at the plant. And there are hundreds or thousands of other things in there that he has found with gas chromatography but not yet identified.

However, there is no need to ditch all your tasty oily foods in a panic. Grob is clear that this is a challenge for analysts, not a worry for consumers. In fact, he's ambivalent about getting media coverage of his project. 'Our philosophy is to inform those really involved and not the consumers, he says. 'It is the authorities that have to do a lot more about this.'

Posted by Emma Marris at 07:09 AM | Permalink | Comments (0) | TrackBacks (0)

In the August 31st issue of Nature, there’s a short ‘picture story’ I wrote about a recent Cell paper from Lee et al. Those authors found that in Trypanosoma brucei (the parasite that causes African trypanosomiasis) the fatty acid myristate is not made by type I or type II fatty acid synthases, but is instead made by a series of enzymes called elongases. These enzymes extend the fatty acid chain, adding two carbon atoms at a time to a fatty acid that is attached to coenzyme A. Though more work is needed to explore how these enzymes function in vivo, the authors believe it may be possible to develop new anti-parasitic drugs that target these elongases.

According to the WHO/TDR, African trypanosomiasis (also known as 'sleeping sickness') affects 36 countries in sub-Saharan Africa and kills about 50,000 people each year. The TDR website says that "[t]reatment has always been difficult, especially when the disease has reached an advanced stage with central nervous system involvement, as few effective drugs are available." So hopefully small-molecule inhibitors of these enzymes could be used to reduce the morbidity and mortality associated with this disease.

If you're interested in reading more about their discovery, please go check out the picture story and the Cell paper.

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 05:30 PM | Permalink | Comments (0) | TrackBacks (0)

- Kosuke Yoshida of Tokai University in Shizuoka, Japan has found a marine microalga, with the handsome name Nannochloropsis oculata, that can be trained to chop the noxious chemical formaldehyde into relatively benign ethyl formate. Yoshida is interested in using the trained strain to mitigate formaldehyde used to control parasites that live on fish gills in aquaculture.

- Hungarian Chemistry celeb George Olah was here yesterday, promoting his new book, Beyond Oil and Gas: The Methanol Economy. He chatted with invitees just a few yards from where he is immortalized on a plaque listing Hungarian Nobel prize winners.

- A chat in the hotel bar with a fellow attendee reveals to ignorant old me that there is such a thing as Philosophy of Chemistry, and that it’s main journal is elegantly named Hyle, after the ancient Greek for “matter”. Further investigation reveals that Nature regular Phil Ball has a paper in the latest edition examining attitudes towards chemists in recent American fiction. The rest of the issue, all about the public image of chemistry is also very interesting. Awesome.

- Mobile phones might be bad for you, especially if your head is a vat of solution of lactoperoxidase, according to Roberta de Carolis of the University of Rome.

- Broccoli sprouts have more glucosinolates—a precursor to cancer-preventing Isothiocyanates—than full grown broccoli.

- The Seine is filled with caffeine and pain relievers.

Posted by Emma Marris at 07:55 AM | Permalink | Comments (1) | TrackBacks (0)

If you read ScientificAmerican.com or the BBC News website this week, you may have heard about Putt et al., which was recently published in Nature Chemical Biology.

Procaspase-3 is an inactive form of caspase-3 (a cysteine protease involved in apoptosis) and the "conversion of procaspase-3 to caspase-3 results in the generation of the active 'executioner' caspase that subsequently catalyzes the hydrolysis of many protein substrates." Putt et al. screened a library of 20,500 compounds and identified a small-molecule - named PAC-1 - that activated procaspase-3 in vitro. They then showed that the small-molecule could induce apoptosis in a variety of cancer cell lines. Since PAC-1 was orally active in live mice and was able to retard tumor growth in three cancer models, the authors believe that this molecule (or its derivatives) could be used to treat cancer in humans one day.

If you want to learn more about the work and you’re attending the fall ACS meeting, Karson Putt will be talking about the work on Tuesday, September 12th in the Medicinal Chemistry Award Symposium. Paul Hergenrother will also be talking in that session (and receiving the award), though he will focus on new small-molecules that might be able to combat Parkinson's Disease.

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 03:58 PM | Permalink | Comments (0) | TrackBacks (0)

Su Doku, the number game that is sweeping the world, has been adapted by the Royal Society of Chemistry into a puzzle where each square must have only one of nine elements listed at the bottom of the page. The play is exactly the same as the digit version, except that one contemplates the likes of lanthanum and cerium while one plays. Check it out at www.rsc.org/puzzle.

Posted by Emma Marris at 08:41 AM | Permalink | Comments (2) | TrackBacks (0)

The big tent where we saw the folk dancers was packed this morning for Jean Marie Lehn's plenary on self-organizing systems. I heard lots of ebullient murmuring on the way out, so I think it went well, though some of it may have been the celebrity-induced glow of those who have just heard a Nobel laureate speak.

The general idea is that if one works hard, one can find molecules that when introduced, get along and immediately start building complex structures on their own. Lehn showed us grids and other cunning structures that had been got up by molecules that recognized each other and then bound predictably.

Much of his work was on those superstructures bound together with metal ions, so that one way to look at his grids was a field of regularly spaced metal ions, potentially useful as a computer chip. So these "supramolecules" are, he said, "a powerful alternative to nanofabrication. Don't make components, design them to make themselves."

He also showed how mixed soups of molecules will segregate themselves into structural units—so you'll have a bunch of double helixes forming alongside a bunch of triple helixes. This relies on recognition, and then selection of the appropriate molecule to fraternize with. In a challenging finale, Lehn wondered if this effect might not represent a kind of "chemical Darwinism."

His other quoteable moment: "Chemistry is the science of informed matter".

Posted by Emma Marris at 08:32 AM | Permalink | Comments (3) | TrackBacks (0)

I heart food chemistry, and for more than one reason. First of all, it is easy to get into the science when you can immediately relate it to cheese or grapes or Parma ham or something nummy like that. And secondly, it demonstrates how seriously we take the pleasure of eating. Much of food chemistry is concerned with ensuring that when we decide to spend an evening eating bon bons and drinking champagne in the bath our chocolate is not adulterated with inferior cocoa butter fat equivalents and our champagne is actually from Champagne.

Elke Anklam, of the European Community Joint Research Centre in Belgium, gave a nice overview of food authentication this morning, which revealed that despite being armed with electronic noses, chromatography of various kinds, spectroscopy ditto., natural isotope fractioning, and PCR, they still can't easily tell if olive oil is being cut with hazelnut oil…"even if you can taste it."

Ha ha! So the best and least scientific means of authentication is still the human tongue. That being said, I was recently informed that most people cannot tell red wine from white with their eyes shut. Incredulous, I put it to the test. I shut my eyes and had my companions at dinner hand me glasses. I called the first red, the second white, and, taking a cue from the snickering I heard, the third a mixture of the two. Turns out it was the same glass of red wine all three times. Oh!

Posted by Emma Marris at 07:55 AM | Permalink | Comments (0) | TrackBacks (0)

If you're an oenophile and you're looking for a job in the near future, you might want to read Corinne Marasco's piece in today's Chemical & Engineering News. As long as you have "strong analytical skills, a good understanding of organic chemistry, and an interest in wine," there might be a job for you in the wine industry.

Lund & Bohlmann wrote a perspective in Science earlier this year, in which they argued that the "art [of making wine] is increasingly guided by science for many wine producers, and this trend will continue with a growing contribution from molecular-based technologies and knowledge." So it might be a good time to (go back to school and) get a graduate degree in Viticulture and Enology.

If you're attending the fall ACS meeting and you want to learn more about the field, you might want to swing by the "Chemistry of Wine" session. Hopefully the speakers will bring along a few bottles for the audience to taste-test...

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 03:31 PM | Permalink | Comments (0) | TrackBacks (0)

Today's programme is chock full of environmental chemistry, including a few sessions on pharmaceuticals in the environment. In the last few decades chemistry has given us more and better drugs, and we have not been shy about taking them. One graph of pharmaceutical consumption in France from 1970 to the present was hair-raisingly steep. All those drugs that aren't broken down by our bodies are, well, let's be scientific here, excreted and enter the waste-treatment stream. Some end up in rivers and lakes.

So it is good that chemists are busy inventing new tools to understand the scope of the problem and what it's implications might be—beyond trout blissed out on Prozac or crustaceans with the caffeine shakes.

Outside the environmental session room, a poster by Mei-Fang Chou and colleagues from Tri Service General Hospital in Taipei, Taiwan, gives me pause. They've managed to tweak the non-speedy alertness enhancer and mood brightener modafinil (sold as Provigil) so that it also is an anti-inflamatory pain reliever. Holey moley—what a blockbuster that could be. A cure for pain, sleepiness and unhappiness in one drug. Look out fish.

Posted by Emma Marris at 09:45 AM | Permalink | Comments (0) | TrackBacks (0)

Mark Peplow, former Nature staffer, and current editor of the Royal Societyof Chemistry's Chemistry World is here in Buda, and he's recording his impressions on a brand new soft-launched blog, which is available here: http://prospect.rsc.org/blogs/cw.

Posted by Emma Marris at 09:09 AM | Permalink | Comments (0) | TrackBacks (0)

Well, the reception was delightful. The food was excellent and the wine got good reviews. But before the eating and drinking came the speeches by chemistry worthies from across the continent. Generally, they were short and expressed pleasure in European chemistry coming together in this conference, and in the umbrella organization, EuCheMS. The MS on the end stands for "molecular science," and is part of a decided emphasis on the molecule which seems to me to be a bit of an attempt to grab more territory for the field.

More inside...

Peter Elvending, the head of the European Chemical Industry Council gave a short presentation on the stiff competition facing its members, especially from the East. The solution, he says, is innovation. "This old continent currently does not stand up to competition," he said. "It is very important that we get our act together in the European Union."

The same sentiment was expressed at a press conference for SusChem, the group of chemical companies, chemists and governments trying to shape the research agenda for Europe. "Commodities will be made elsewhere," said Alfred Oberholz, head of the scheme, "we must have innovation and sustainability."

The research the group thinks is worth doing will cost 1,400 million euros a year, half to be supplied by governments and half by industry. I am not sure yet how that compares to the current figures. Their goal is to get the plan linked into the EU's Seventh Framework Programme, which is no doubt being hammered out in smoke-filled rooms even as we speak.

If you want to see if your pet project is one of the SusChem fave raves, check out their draft at http://www.suschem.org/.

Oh, one last thing about the reception: it's one thing to present musicians in Hungarian costume and young men in tight crimson trousers pirouetting with gals decked out like the St. Pauly girl, but give your guests a drink before rather than after.

[reprinted from the Nature Newsblog - see all reports from the congress here: http://blogs.nature.com/news/blog/conference_reports/european_chemistry_congress/]

Posted by Emma Marris at 07:59 AM | Permalink | Comments (0) | TrackBacks (0)

Jó napot kívánok from Budapest, where the European chemistry community has decided to get together in the first ever European Chemistry Congress. The scale of the thing is impressive for it being a first: 2,500 registrants from 65 countries and an abstracts book the size of a phone book (do they still make those?).

Before the official start, I sat down with organizer Gábor Náray-Szabó, and asked him the obvious question: is this conference a challenge to the American Chemical Society meeting, that twice-annual mass migration of chemists?

Click below to read on...

"They do it very well," says Náray-Szabó. "We don't have to fight. But we can show that we can do something like that."

Náray-Szabó says that the time seemed ripe for European chemists to come together. The meeting has been taking shape for the last several years, but a turning point, he says, is when Jean-Marie Lehn signed on to give a plenary talk and help develop the programme. More Nobel laureates followed. Right now, Náray-Szabó is confident of the congresses success, and it looks like others chare his confidence. The Societá Chimica Italiana will host the next one in Torino in 2008. I withhold my vote until after the opening reception. Will there be adequate nibbly things and drinks? Will the chatter be lively?

Right now, the exhibitors are setting up, and everywhere knots of people are huddled, pouring over the dense program. Young people in pale blue polo shirts are registering people at a furious pace, and the Eötvös Loránd University chemistry building, on the bank of the Danube, smells strongly of newly printed programs. If only one could absorb all the presentations just by breathing in that inky smell!

[reprinted from the Nature Newsblog - see all reports from the congress here: http://blogs.nature.com/news/blog/conference_reports/european_chemistry_congress/]

Posted by Emma Marris at 01:23 PM | Permalink | Comments (0) | TrackBacks (0)

In the September issue of Nature Chemical Biology, John Silvius wrote about McGill University's interdepartmental graduate program in chemical biology, which was established in 2002 and now has "roughly 30 graduate students, 10 postdoctoral fellows and 30 faculty mentors."

The program involves scientists from the Department of Biochemistry, the Department of Chemistry, and the Department of Pharmacology and Therapeutics, and a "key objective of the program is to maximize opportunities for students with chemistry and life science backgrounds to share and appreciate their sometimes distinct perspectives on the field of chemical biology." Silvius wrote that this is accomplished via seminar discussion meetings, workshops, and an "annual research symposium at which students present their work to other students and faculty mentors."

There are other interdepartmental and multi-institutional graduate programs in chemical biology: for example, there is the Cornell/Rockefeller/Sloan-Kettering Tri-Institutional Training Program in Chemical Biology in New York City (which involves Cornell University, The Rockefeller University, Memorial Sloan-Kettering Cancer Center, and the Weill Medical College of Cornell). Graduate students in the Tri-Institutional Training Program can rotate in (and join) laboratories at any of the institutions and they do not have to teach classes, "enabling them to take an accelerated course schedule (four courses per semester during the first year)." (Although I understand that the program was designed so the students could take a large number of classes, I really enjoyed teaching during graduate school and think it's an important experience for all graduate students. But I'll save that topic for another blog post...)

There's obviously more than one way to train the next generation of chemical biologists, but Silvius believes that

An effective training program in chemical biology must produce graduates who have a distinct sense of intellectual identity yet can work effectively with researchers that are more conventionally trained either in chemistry or in the life sciences alone... Moreover, by promoting constant intermixing of individuals trained in the cultures of chemistry and biology, such a program allows students to be participants in the very type of stimulating, creative ferment that drives the field of chemical biology itself.

If you are a graduate student in (or a recent graduate of) an interdepartmental or multi-institutional graduate program in chemical biology, I'd be interested in hearing your thoughts about your program/your experiences. Why did you choose an interdepartmental or multi-institutional graduate program, instead of a Department of Chemistry & Chemical Biology? (And for those of you who did their graduate work in a Department of Chemistry & Chemical Biology, why didn't you choose an interdepartmental or multi-institutional graduate program?) For those of you working on the interface of other disciplines (for example, biophysics, chemical physics, bionanotechnology, etc.) did your graduate program meet your (scientific) needs/expectations? If not, what could they have done to make it easier for you to pursue interdisciplinary research?

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 10:31 AM | Permalink | Comments (4) | TrackBacks (0)

On the train home last night I was directed to an article in The Guardian about the state of chemistry and physics education in the UK. (It's a shame that the picture accompanying the online version is nowhere near as amusing as the one in the actual newspaper - it was your stereotypical wild-hair crazy-professor type, complete with labcoat, standing in front of a blackboard covered with chemical structures and even the mechanism of ester hydrolysis... base-catalysed just in case you were wondering).

One of my favourite passages is the following:

Add to the old stereotypes new ones about shortening attention spans and a rise in the need for instant gratification and it starts to look as if, while sticking a splint in a bunsen burner or watching magnesium combust might have swung things in the old days, these days it just won't do.

I wonder if I'd had an XBOX whether I would have been so excited about a bit of sodium whizzing around in a beaker of water; all those flame tests with different colours probably wouldn't have been all that captivating either...

If you have a few minutes to spare, go and have a read and ponder on who should be the Jamie Oliver (link included for the last few people on Earth who don't know who this is) of chemistry?!

Stuart

Stuart Cantrill (Associate Editor, Nature Nanotechnology)

Posted by Stuart Cantrill at 06:34 AM | Permalink | Comments (1) | TrackBacks (0)

You might remember endosymbiotic theory from your high school or college biology classes: it's the idea that some organelles (for example, mitochondria and chloroplasts) were originally separate prokaryotic organisms that were engulfed by eukaryotic cells. Although it's not clear how or why this occurred, this became a mutually beneficial relationship for both cells (i.e., a symbiotic relationship), resulting in the organelle-containing cells that appear in biology textbooks (and in our bodies...)

But why - you might ask - would a chemist care about endosymbionts (organisms that live inside other organisms)? Well I think they're interesting because "[b]acterial symbionts have long been suspected to be the true producers of many drug candidates" isolated from natural sources. For example, there is some evidence that the antitumor polyketides of the pederin family are produced by an uncultured bacterial symbiont of Paederus beetles, which can cause dermatitis.

Late last year, Partida-Martinez & Hertweck discovered that another natural product (rhizoxin) is not biosynthesized by the fungus Rhizopus microsporus itself, but by a bacteria that lives inside the fungus. In a follow-up paper in JACS, these authors were able to isolate a rhizoxin-producing bacterial strain from the fungus ("Burkholderia rhizoxina") and could grow it in liquid culture. They lysed the cells, and found (quite surprisingly) that "about 40% of the crude extract is composed of rhizoxin derivatives" - in addition to rhizoxin, Burkholderia rhizoxina produces a number of related structures.

The authors determined that some of these natural products were 1,000 to 10,000 times more active than rhizoxin in cell-based assays (the assay was looking at antiproliferative activity). Rhizoxin went through extensive clinical trials in the 1990s and showed some promise as an anti-cancer drug, though it was not taken into Phase III clinical trials because it was not active enough in vivo. These authors hope that, since the derivatives they isolated are more active in vitro, they might more successful in the clinic. And since the natural products can be harvested from bacterial cultures, it may be possible to rapidly produce a large amount of these complex natural products without having to resort to chemical synthesis.

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 11:30 AM | Permalink | Comments (0) | TrackBacks (0)

I’ve just gotten home from the 20th Protein Society meeting in San Diego where, I have to say, I was completely overwhelmed by the quality of the talks I saw. I was also overwhelmed by the beautiful weather, and I frequently found myself asking why I (and everyone, in fact) don’t move to San Diego immediately. One thing that could be keeping people away is the creepy way that the hotel staff use your name when you’re wearing your nametag (‘Here’s your hot chocolate, Catherine!’ … Augh!).

Unlike some of Hollywood's recent offerings, there were several movies that got my attention during the meeting. One was in a talk by Ron Milo, who is incorporating fluorescent proteins into human genes with retroviruses to monitor what individual proteins are doing and, on a larger scale, assess variability in a population of cells. While not really movies, both Vijay Pande and Dave Baker gave demonstrations of their community-based computational projects, Folding@home and Rosetta@home. While I'm familiar with Baker's work in protein design, this was my first time seeing him talk; all I can say is that I'm starting a countdown to when he wins the Nobel Prize. Pande's talk on protein folding assessed by multiple short simulations instead of one long computational run impressed as well in his acceptance of the Irving Sigal Young Investigator Award. Tim Springer never fails to entertain with his integrin signaling interpretive dance (to clarify: he's not the one dancing). I've seen the movie before on his web page, but seeing it in the context of the whole talk was excellent. Finally, Barbara Imperiali demonstrated the power of caged phosphorylation sites in preventing/facilitating cell migration.

As a result, I would like to send this letter on to all involved in the movie enterprise (or at least the recent offering from Samuel Jackson and company):

Dear Hollywood,
I think you can do better.

Sincerely,
Catherine Goodman (Assistant Editor at Nature Chemical Biology)

Posted by Catherine Goodman at 02:43 PM | Permalink | Comments (0) | TrackBacks (0)

As a follow-up to yesterday's post, I took a look at Wikipedia's 'List of Chemists': all the Nobel laureates have entries (for example, EJ Corey, Barry Sharpless, Ahmed Zewail, etc.) and though the top of the page boldly claims 'This is a list of famous chemists: (alphabetcal [sic] order),' this is by no means a fleshed out list of 'important' chemists: Margaret Thatcher is on the list, but George Whitesides didn't make the cut for some reason. (I don't mean any disrespect to the former Prime Minister, but I don't think many scientists think 'oh yeah, she's a chemist' when they hear her name...)

Whether you like it or not, Wikipedia has become the first place many people look to find information (online). But the information on chemists isn't up to snuff: as I mentioned, George Whitesides has an entry, but a number of other respected chemists in the same chemistry department don't appear in Wikipedia (for example, Eric Jacobsen, Andrew Myers, Eugene Shakhnovich, and David Liu, just to name a few...)

So I had a thought - let's flesh these Wikipedia entries out...

If you have time in the next week, add an entry for your Ph.D./post-doc supervisor, one of your co-workers (if you're a professor), or someone whose work you've enjoyed reading for years. If they already have an entry, add some (truthful) information to it... And if you add their names to the 'List of Chemists,' don't forget to put them in 'alphabetcal' order...

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 10:54 AM | Permalink | Comments (1) | TrackBacks (1)

A few nights ago I was talking with my wife about fame (i.e., what makes someone a 'superstar') - it's pretty easy to understand why so many actors/actresses, musicians, and writers are household names (whether or not you like Ben Affleck or Shakira, many people know who they are...) The average person might not be able to name a living artist or dancer, though I bet a number of people would say "Christo and Jeanne-Claude" and "Baryshnikov"...

But if you asked the average person to name a famous living chemist, I wonder if they could name anyone... (This is probably not true in Japan, since Nobel laureates have a unique "celebrity status," but in most other countries I wonder what the average person would say...)

So the million dollar question is can anything be done about this? (A related question is should anything be done about this, but for the sake of argument, I'm going to assume that something should be done about this...) Movies are certainly the easiest way to inform the general public: Awakenings, A Beautiful Mind, and Kinsey helped popularize the names "Oliver Sacks," "John Nash," and "Alfred Kinsey."

So do we need a movie about Barry Sharpless? Or, as someone suggested on "In the Pipeline," should The Billion Dollar Molecule be made into a movie? I don't know about you, but I'd watch a movie about RB Woodward - from all the stories I've heard, he sounded like an interesting guy...

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 10:03 AM | Permalink | Comments (7) | TrackBacks (0)

The 'front half' of this week's Nature is packed full of chemistry - there's a News & Views by Tom Muir on a recent JACS paper from David Liu's group, Emma Marris wrote a short News piece on the controversy surrounding two recent syntheses of hexacyclinol, and Phil Ball wrote a News Feature on the big questions facing chemistry (or in his own words: "are there still major chemical questions to crack?")

In 2005, Science published a special issue that featured 125 'big questions' that scientists hope to solve in the next 25 years - some of the chemical questions included 'How far can we push chemical self-assembly?,' 'What is the structure of water?,' and 'Are there limits to rational chemical synthesis?'. Phil adds a few more questions to the list, including 'How do we design molecules with specific functions and dynamics?' and 'What is the chemical basis of thought and memory?'.

Let's say you had a lab of 20 highly competent graduate students and post-docs and was just awarded a large grant (how about one million dollars per year for five years - wouldn't that be nice...) What problem(s) would you work on? Would you tackle a basic/fundamental problem or use chemistry to explore an interesting biological system, make new materials/devices, develop new therapeutic agents, or something other application?

Joshua

Joshua Finkelstein (Associate Editor, Nature)

Posted by Joshua Finkelstein at 08:39 AM | Permalink | Comments (2) | TrackBacks (0)

In the editorial in August’s Nature Chemical Biology, we share our thoughts on peer review. As you can imagine, the exact timing of an editorial on this topic coincides with the peer review trial and debate going on over at Nature, but the thoughts within the article (as well as many related ideas) are frequently on our minds. My most recent inspiration, however, comes from a trip to a convenience store to buy some toothpaste. The veritable cornucopia of choices (even within a single brand!) made me wonder: if we need 50 different kinds of toothpaste to satisfy what seems a fairly simple concept (of cleaning our teeth), how will we, in the face of an equally overwhelming number of choices, ever come to an agreement on a system as complex and important as peer review? I guess one comforting thing is that until we can figure out a better way to conduct this process, our current method seems to be working pretty well.

Some major questions on our minds:

How do we make sense of all the different options being proffered as changes to the current peer-review system?

How long do new ideas need to be tested before we agree that they are better or worse than the current system?

Is it a reasonable expectation that scientists make time to referee papers on a voluntary basis, as is being explored in the Nature trial?

How would we prevent scientists from encouraging their friends to submit overly positive reviews?

What rewards could/should there be for acting as a referee?

Can/does science exist outside of a political environment, where professors need to worry about the good opinion of their peers?

Obviously, this topic is of great significance to us, and we have many ideas of what the answers to these questions could be. But we already know what we think about it - tell us your thoughts!

Catherine (Assistant Editor, Nature Chemical Biology)

Posted by Catherine Goodman at 04:42 PM | Permalink | Comments (2) | TrackBacks (0)

Channel 5 in the UK has been running a series of documentaries with a ‘Stranger than Fiction’ theme. Based upon the promos, which generally made me turn away from the TV and go ‘eew’ (especially the one about head transplants), I’ve steered clear of them... until last night.

“Death in the deep freeze” was about cryonic preservation – freezing bodies (or just the head if you prefer) post mortem* in the hope that future technology can (1) thaw you out, (2) re-animate you, and (3) cure whatever it was that shuffled you off this mortal coil in the first place. Most of the debate was about point 1 and whether you can freeze complex biological systems and then thaw them out so that they still work. As for point 2, I saw many bad science-fiction films about that when I was a teenager. Point 3 seems reasonable; advances in medicine will almost certainly enable us to cure diseases in the future that are not treatable at the moment. The problem is, 3 only becomes relevant in the context of cryonics if 1 and 2 can be sorted out.

(*Apparently, the definition of death comes in to play here – a cryonics ‘patient’ is legally dead, but the proponents of this technology claim that they remain ‘biologically alive’. The programme last night showed the vitrification process in full, including the chest being cracked open and a pretty big drill making its way into the skull – if they do manage to bring anyone back they’re bound to have quite a headache. For more information, go to Alcor's website).

According to the programme, the freezing and successful thawing of organs has been demonstrated with rabbit kidneys - the goal of this research, however, is to increase the amount of time an organ can be stored before being transplanted. It’s still quite a stretch from there to being able to freeze Thumper whole and then expecting him to munch away on carrots when you warm him up again.

Anyway, why do I bring this up? Well, this was my first public sighting of nanotechnology for some time. According to Ralph Merkle, a professor at the Georgia Institute of Technology, nanotech theorist and Alcor director, future medicine based on molecular nanotechnology may be the answer. The programme contained wonderful animations of nanobots with Merkle telling us that trillions of them could be used to manipulate the molecules in frozen tissue to restore them back to health. Whether you think the whole process may be plausible or not, Merkle has a great ‘payoff matrix’ on his website which reduces the debate to its most simple form.

Stuart

Stuart Cantrill (Associate Editor, Nature Nanotechnology)

Posted by Stuart Cantrill at 12:55 PM | Permalink | Comments (0) | TrackBacks (0)