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Archive for December, 2012


An end of the year tradition is to get the bad stuff out of the way, so that the New Year can be ushered in without contamination by the bad (this includes cleaning the house!). Apparently (like choosing the right person for “first footing”) this brings good luck, though personally, I think that stochastic processes rule and so there is nothing special about any particular day. Nonetheless, traditions are what bind us culturally, so onwards with the “bad”.
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One point made in , a posting by Raphael on the lack of evidence for stripes on nanoparticles is the duplication of data between
Figure 2 in Chem Comm 2008, 196 and Figure 1 in Nat Mater. 2008 (7):588-95

What is most surprising is how little comment such duplication has raised.
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With a past PhD student of Francesco Stellacci’s, Predrag Djuranovic, weighing in to the debate, I think there are some important questions and some interesting observations that should be made. (more…)

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I have been prompted to write this post following a number of unrelated events two of which are:
(1) Comments on Raphael’s blog “Stripy nanoparticles revisited” post.
The comment, by Someone has to say it, states that one is either a scientist or a blogger. I would note that of all the comments, this is the only one that is not civil and borders on Trolling. However, if we take this comment at face value, then we have a simple statement to consider: “Blogging is not science?”

(2) Continued comments on Science Fraud.
A veritable litany here. Not always civil, but the blogger doubtless has a lot of Trolls to put up with. Just to take one recent example, commenter “John” (and here) makes in essence a similar point to “Someone has to say it” and, moreover, argues that the fact that Science Fraud is entirely anonymous detracts from the validity of its postings. (more…)

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LT1 at 1 pm
Prof Dave Allsop from Lancaster University will give a seminar entitled “Protein oligomers as toxins, biomarkers and molecular targets for neurodegenerative disease”

Buffet lunch will be available in the Committee Room from 12 noon.

The formation of fibrillar aggregates from a range of different proteins is a common feature of numerous different ‘protein conformational’ diseases. In these diseases, normally soluble proteins are deposited in the form of insoluble fibrils inside and/or outside of cells. In the systemic amyloidoses, extracellular fibrillar deposits (often called amyloid) can be found in many different tissues and organs throughout the body. Localised deposits are found in some other diseases, such as late-onset diabetes, where they are restricted to the pancreas, and some important neurodegenerative diseases, where they are often found only in the brain. Examples of the latter include Alzheimer’s disease, Parkinson’s disease, the prion diseases (e.g. CJD in humans), Huntington’s disease, frontotemporal dementia and motor neuron disease. David’s  research is concerned with the pathological role of these misfolded proteins, and is focussed mainly on neurodegenerative disease and late-onset (type 2) diabetes.

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Professor Philip Moriarty from the University of Nottingham, who is a specialist in scanning probe microscopy, especially STM, has weighed in with an opinion. It should be stressed that this is entirely external and so is most welcome. As he points out, other analyses, e.g., 2-D NMR, may or may not hold up the hypothesis. This reinforces my earlier call for specialists in the different measurement modalities used to measure the orgnisation of ligands on the nanoparticle surface to bring their expertise to bear.

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