Chemistry Blog needs you!

Poor old chemistry-blog, its being going since 2006, but its been a bit neglected of late. So as it approaches it’s teenage years, (13 in May!) we felt it could do with a new lease of life.

So we’re blowing the dust off the old thing and inviting a new generation of writers, chemists and chemistry enthusiast to join the venerable network.

If you fancy contributing to the site then drop us a line (email, twitter or the comments are fine) and let us know why you’d like to write for the blog and a little bit about your background (280 characters will do!).

Over the years we’ve covered  everything from data manipulation, plagiarism to a fair bit of larking around.  In case you need any reminders here’s a few of our highlights (in no particular order, and having polled exactly one person).

Over to you!

The Rules

Alleged Data Manipulation in Nano Letters and ACS Nano from the Pease group

What’s in Lemi Shine? – UPDATED

Something Deeply Wrong With Chemistry


  1. I’d also like to add, that we will be fixing the template soon. We ran into an issue when updating to the latest most secure version of WordPress. It’ll take a couple of days to work through.

  2. I write my own blog, but feel free to include my posts.


    Here’s an example — more biochemical and molecular biological then chemistry, but chemistry is at its core.

    A research idea yours for the taking

    Why would the gene for a protein contain a part which could form amyloid (the major component of the senile plaque of Alzheimer’s disease) and another part to prevent its formation. Therein lies a research idea, requiring no grant money, and free for you to pursue since I’ll be 80 this month and have no academic affiliation.

    Bri2 (aka Integral TransMembrane protein 2B — ITM2B) is such a protein. It is described in [ Proc. Natl. Acad. Sci. vol. 115 pp. E2752 – E2761 ’18 ]

    As a former neurologist I was interested in the paper because two different mutations in the stop codon for Bri2 cause 2 familial forms of Alzheimer’s disease Familial British Dementia (FBD) and Familial Danish Dementia (FDD). So the mutated protein is longer at the carboxy terminal end. And it is the extra amino acids which form the amyloid.

    Lots of our proteins form amyloid when mutated, mutations in transthyretin cause familial amyloidotic polyneuropathy. Amylin (Islet Amyloid Polypeptide — IAPP) is one of the most proficient amyloid formers. Yet amylin is a protein found in the beta cell of the pancreas which releases insulin (actually in the same secretory granule containing insulin).

    This is where Bri2 is thought to come in. It is also found in the pancreas. Bri2 contains a 100 amino acid motif called BRICHOS in its 266 amino acids which acts as a chaperone to prevent IAPP from forming amyloid (as it does in the pancreas of 90% of type II diabetics).

    Even more interesting is the fact that the BRICHOS domain is found in 300 human genes, grouped into 12 distinct protein families.

    Do these proteins also have segments which can form amyloid? Are they like the amyloid in Bri2, in segments of the gene which can only be expressed if a stop codon is read through. Nothing in the cell is perfect and how often readthrough occurs at stop codons isn’t known completely, but work is being done — Nucleic Acids Res. 2014 Aug 18; 42(14): 8928–8938.

    I find it remarkable that the cause and the cure of a disease is found in the same protein.

    Here’s the research proposal for you. Look at the other 300 human genes containing the BRICHOS motif (itself just a beta sheet with alpha helices on either side) and see how many have sequences which can form amyloid. There should be programs which predict the likelihood of an amino acid sequence forming amyloid.

    It’s very hard to avoid teleology when thinking about cellular biochemistry and physiology. It’s back to Aristotle where everything has a purpose and a design. Clearly BRICHOS is being used for something or evolution/nature/natural selection/the creator would have long ago gotten rid of it. Things that aren’t used tend to disappear in evolutionary time — witness the blind fish living in caves in Mexico that have essentially lost their eyes. The BRICHOS domain clearly hasn’t disappeared being present in over 1% of our proteins.

    Suppose that many of the BRICHOS containing proteins have potential amyloid segments. That would imply (to me at least) that the amyloid isn’t just junk that causes disease, but something with a cellular function. Finding out just what the function is would occupy several research groups for a long time. This is also where you come in. It may not pan out, but pathbreaking research is always a gamble when it isn’t stamp collecting.

  3. Sir Thanks for sharing amazing information

  4. Sir thanks for sharing this information

  5. As you said it is very useful and helpful for chemists and chemistry enthusiast writers. Thanks to get back again after so years

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