Feeds:
Posts
Comments

Posts Tagged ‘protein chemistry’


Gel (see footnote at end for a brief description of gels aimed at non-biologists) splicing is a term that describes the cutting and pasting of images of lanes (where 1 lane = 1 sample) and placing the images of the lanes in a different order or even combining lanes from different gels. A more extreme form is to simply shift the subsection of the lane, corresponding to the probed molecule, from one lane to the next.
This is wrong and it always has been. However, in post publication peer review on PubPeer, it is often defended, particularly for “older” papers, from a decade or more ago. This then raises arguments about what was acceptable then and are we shifting the goalposts of scientific integrity? The matter has even been a “Topic” on PubPeer. (more…)

Advertisements

Read Full Post »


Changye and Yong’s first paper, up as a preprint at PeerJ
in accord with my 2015 and 2014 New Year resolutions describes an accidental discovery. One of their co-authors, Sarah Taylor, was exploring HaloTag as an alternative means of labelling protein to green fluorescent protein, and I thought it would be good to be able to have a pure in vitro system to validate labelling. So Changye and Yong made some recombinant HaloTag fibroblast growth factor-2 (HT-FGF2). When they showed me the gel, they noted that HT-FGF2 did not seem terribly promising, because there was quite a lot of protein in the bacterial pellet.

It is at this point that the professor earns his keep, (more…)

Read Full Post »


Dan Nieves’ paper on an easy and accessible method to covalently conjugate proteins, sugars and indeed pretty much any biomoleucle onto nanoparticles has just come out in Chem. Commun. (more…)

Read Full Post »


This post is entirely inspired by a Tweet that appeared in my stream via @stuartcantrill, a request for ideas on the future of chemistry. My (instant) response was that we have to replace everything with materials derived from waste biomass. After finishing my morning check of information systems and my coffee, it was time to get on my bike and cycle to the university. This set off the lateral neuronal activity that my brain engages in when I cycle – the worse the traffic, the more lateral activity… (more…)

Read Full Post »


Kat’s paper on the interactions of neuropilin-1 with a heparan sulfate mimetic library of modified heparins is now published in The PeerJ
(more…)

Read Full Post »


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.

Read Full Post »