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Chemistry World April 2009 Philip Ball	Column: The crucible Unwinding protein fibrils could give a glimpse of how peptides survived on early Earth
Chemistry World March 16, 2014 Simon Hadlington	Short peptides self-assemble into a catalyst Researchers in the US have created catalysts from peptide chains that are only seven amino acids long.
Chemistry World September 12, 2014 Hayley Simon	Coated nanoparticles show Alzheimer's promise Nanoparticles coated in an amino acid polymer have been found to prevent the formation of amyloid fibrils -- incorrectly folded protein fibers associated with the development of neurodegenerative diseases.
Chemistry World June 14, 2009 Hayley Birch	New technique probes Alzheimer's aggregates US and UK researchers have used a new technique to identify what they think could be the primary toxic species in the development of Alzheimer's disease
Chemistry World June 17, 2012 Jon Evans	Anti-social amino acids gang up Previously thought to be purely the preserve of proteins and peptides, scientists have discovered that the amino acid phenylalanine can form the toxic amyloid fibrils that are a hallmark of diseases such as Alzheimer's and Parkinson's.
Chemistry World October 27, 2014 Tim Wogan	Folding rules used to build unnatural proteins Scientists in the UK and US have designed and synthesized unnatural protein structures, using theoretical calculations to explore the factors affecting protein folding and stability.
Chemistry World February 13, 2014 Philip Ball	Ice core to antifreeze protein's inner workings The antifreeze protein that protects the winter flounder from sub-zero temperatures has been found to have an odd structure.
Bio-IT World June 12, 2002 Karen Hopkin	Computational Biologists Join the Fold CASP5 competitors compare the best algorithms for modeling the 3-D structure of proteins -- an exercise that could lead to new insights into the pathogenesis and treatment of disease.
HHMI Bulletin Fall 2012 Halleh B. Balch	Like a Chinese Finger Trap In neurodegenerative diseases like Alzheimer's, the needle-like fibers that accumulate in the brain are not the real damage-doers. The culprits are intermediate protein structures, called small amyloid oligomers, made of a few proteins that misfold and aggregate.
Chemistry World September 29, 2010 Hayley Birch	Protein folding: knotted or not A new study may help scientists unravel the complex problem of protein folding. The study suggests knotted proteins, which present a particular challenge to folding experts, could be untied with a couple of well-targeted tugs.
Chemistry World April 29, 2013 Caryl Richards	Protein origami sets scene for designer structures A world first in the art of protein origami has been attained with a novel method of folding a polypeptide chain into a three-dimensional tetrahedron.
Chemistry World November 15, 2010 Manisha Lalloo	pH prompts protein structure US researchers studying the naturally-occurring amyloid protein Pmel17 have discovered that pH plays an important role in its structure, helping the body control its aggregation.
Chemistry World March 4, 2011 Russell Johnson	Tracking the early stages of Alzheimer's disease UK researchers can track the early steps of formation of peptide clumps linked to Alzheimer's disease using the peptide's fluorescent ability. This could help design effective therapies for the disease at an early stage.
Chemistry World April 30, 2007 Victoria Gill	Amyloid Protein Seen to Zip Together Amyloid proteins' long, complicated structure makes them tricky to study, but U.S. researchers have found that they share a common feature that could provide a drug target for an array of incurable conditions.
Chemistry World December 10, 2009 Phillip Broadwith	Solving fibril formation "It really is a case of the ideas of mathematics and physics helping us to understand chemistry and biology," says Chris Dobson of the University of Cambridge.
Chemistry World November 27, 2013 Jennifer Newton	A cytochrome from scratch Artificial proteins could be closer to participating in natural biochemical pathways after researchers show that bacteria will process amino acid sequences entirely unrelated to any natural protein to produce a fully functioning cytochrome.
Prepared Foods February 2008 Sharon Book	Article: Protein Ingredients for Health and Texture A variety of soy, dairy and egg proteins are available for the food formulator to obtain the desired texture in a food or beverage.
HHMI Bulletin Feb 2012	An Intentional Life Scientists have identified a number of genes associated with familial forms of ALS, and Arthur Horwich has homed in on one of them.
Bio-IT World June 12, 2002 Mark D. Uehling	Putting Proteins in Their Place Will a 'periodic table' of proteins help classify the ungainly beasts?
Chemistry World May 12, 2010 Phillip Broadwith	Tying up spider silk's loose ends The way spider silk proteins can be stored as a fluid but spun instantly into fibres is all down to their end parts, European scientists have discovered.
Chemistry World December 21, 2006 Henry Nicholls	Silent SNPs Serve up a Structural Surprise The sequence of amino acids no longer dictates the structure and function of a protein according to a surprising new paper.
Chemistry World November 20, 2013 Rebecca Brodie	Therapeutic screening for Alzheimer's disease Scientists in Canada and the US hope a system they have developed for monitoring amyloid- aggregation on a chip could be used to find new treatments for Alzheimer's disease.
Chemistry World February 3, 2013 Andy Extance	Enzyme draws nanopore protein sequencing nearer US scientists at the University of California, Santa Cruz, have made a key step towards nanopore protein sequencing, thanks to an 'unfoldase' enzyme. Mark Akeson's team exploited this enzyme to unravel proteins and pull them through nanopores.
HHMI Bulletin May 2010 Lauren Gravitz	Live Long and Prosper Mix amyloid plaques with longevity and you get mice that not only live longer, but healthier too.
Chemistry World July 30, 2008 Sarah Houlton	A metal trap to stop Alzheimer's Trapping metals could prove a key to curing Alzheimer's disease, according to the promising results of early clinical trials on a compound called PBT2.
HHMI Bulletin May 2010 Richard Saltus	A Silver Lining Sure, some prions can cause diseases, but others are turning out to be beneficial.
Chemistry World June 2009 Michael Gross	Bubble-wrapped frogs Tropical frogs create remarkable protein foams to protect their spawn. Exploration of the underlying chemistry has only just begun
Chemistry World April 27, 2006	`Sticky Trees' Glue Molecules to Proteins Researchers have developed a chemical glue that binds molecules to proteins without compromising protein function. The method could be used to modify a wide range of proteins for a variety of purposes, such as in the development of new protein-based therapies.
Chemistry World June 1, 2012 Simon Hadlington	Protein architecture with atomic precision Researchers have made a key breakthrough in designing and building geometrically defined nanostructures from proteins with unprecedented accuracy.
Chemistry World July 20, 2012 Michael Parkin	New supramolecular Alzheimer's drugs Supramolecular chemistry could provide a new avenue in the treatment of Alzheimer's disease, say scientists in China.
Reactive Reports Issue 51 David Bradley	Protein Crystals Trapped Researchers have developed a new technique for crystallizing proteins, which could open up a whole range of materials to this powerful analytical technique.
Chemistry World August 26, 2008 Fred Campbell	High-throughput protein microarrays on the way A new method to rapidly generate protein microarrays has been developed by UK researchers at the University of Manchester.
Chemistry World May 5, 2010 Mike Brown	Natural artificial muscles Scientists in Canada and the US have developed artificial proteins that mimic the elastic and mechanical properties of the muscle protein, titin.
Chemistry World December 9, 2013 James Urquhart	Drug fix for misfolded proteins promises hope for incurable diseases Researchers have been looking into pharmacological chaperones or pharmacoperones. They might treat diseases brought about by genetic mutations that cause otherwise functional proteins to become misfolded or misrouted.
Chemistry World June 19, 2012 Anthony King	Nanoparticles linked to rheumatoid arthritis Three types of nanoparticles were found to ramp up protein citrullination in cell cultures, a change that can make the body think native proteins are foreign. This process has previously been linked to autoimmune disease.
Pharmaceutical Executive November 1, 2006	Thoughtleader: Making Things Stick Ambrx has created the "glue" that allows researchers to attach activity-enhancing molecules to amino acids where they couldn't before.
Chemistry World July 31, 2012 David Bradley	Hydrogels can release drugs one at a time A hydrogel that can be programmed to release different protein drugs one after the other rather than all at once could simplify the delivery of complex therapeutic regimens for various diseases.
Chemistry World November 13, 2014 Katrina Kramer	Persuading proteins to form porous polyhedra Researchers in the US have designed a hollow cube out of naturally occurring proteins, something that was previously only possible with DNA.
Chemistry World July 6, 2007 Michael Gross	Predicting How Proteins Fold Researchers in Italy and the UK have now developed a computational approach that can simulate the folding of membrane proteins in atomic detail.
HHMI Bulletin February 2011 Michele Solis	Right Before Your Eyes Coupling protein sequence to function, thousands of variants at a time.
Technology Research News January 14, 2004	Wet biochip preserves proteins Researchers from Kyushu University in Japan have produced a hydrogel material that makes it possible for proteins to survive aboard labs-on-a-chip.
Chemistry World October 24, 2008 Hayley Birch	Proteins swap partners UK researchers have discovered that proteins which use metal cofactors can be surprisingly promiscuous metal binders, happily taking up the 'wrong' metal.
Bio-IT World October 10, 2003 Jeffrey Skolnick	Protein Structure Prediction in Drug Discovery Indications are that structure prediction can assist in the automated assignment of proteins to known pathways.
Technology Research News September 24, 2003 Kimberly Patch	Heated plastic holds proteins One important task for biochips is sorting proteins, but it's tricky business getting protein molecules to be where you want them and stay away from where you don't. A tiny, plastic-coated hot plate allows scientists to trap and release proteins on command.
Chemistry World June 14, 2011	A New Spin on Protein NMR A new technique will allow researchers to study protein structure in greater detail using NMR.
Bio-IT World December 10, 2002 Kevin Davies	Do Try This @ Home In the most impressive sign of distributed computing's awesome potential in biology thus far -- at least in peer-review literature -- researchers have simulated the folding of a mini-protein on a microsecond timescale.
Chemistry World December 12, 2011 Simon Hadlington	Zwitterion approach to stabilizing drug proteins Researchers in the US have discovered a new way to stabilize and protect protein molecules without affecting the protein's biological activity.
Chemistry World October 27, 2006 Richard Van Noorden	Synthetic Origami Folds Like Natural Enzymes Researchers have synthesised a large organic molecule that folds up like a small protein, though its backbone is entirely non-biological. The achievement is a step along the path to producing truly synthetic enzymes in the laboratory.
Reactive Reports September 2005 David Bradley	When Good Turns Bad Prions, the protein-like pathogens at the heart of the fatal brain disorder CJD, so-called mad cow disease, and related diseases can rapidly "remodel" good proteins into bad, according to US scientists, who have demonstrated this for the first time in living cells.
Chemistry World May 9, 2007 James Mitchell Crow	Controlling prion folding US scientists report that prions, infamously linked to mad cow disease, have crucial subsections that control their behavior, including whether or not they can cross between species.