One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

Several hereditary neurological and neuromuscular diseases are caused by an abnormal
expansion of trinucleotide repeats. To date, there have been 10 of these trinucleotide repeat …

Huntington's disease is a genetic neurodegenerative disorder resulting from polyglutamine
(polyQ) expansion (> 36Q) within the first exon of Huntingtin (Htt) protein. We applied X-ray …

Aggregation of proteins containing polyglutamine (polyQ) expansions characterizes many
neurodegenerative disorders, including Huntington's disease. Molecular chaperones …

The progress toward understanding the molecular basis of Alzheimers's disease is strongly
connected to elucidating the early aggregation events of the amyloid-β (Aβ) peptide …

Huntington disease (HD) is caused by an expansion of more than 35–40 polyglutamine
(polyQ) repeats in the huntingtin (htt) protein, resulting in accumulation of inclusion bodies …

Two serine residues within the first 17 amino acid residues of huntingtin (N17) are crucial for
modulation of mutant huntingtin toxicity in cell and mouse genetic models of Huntington's …

The 17-amino-acid N-terminal segment (httNT) that leads into the polyglutamine (polyQ)
segment in the Huntington's disease protein huntingtin (htt) dramatically increases …

Polyglutamine (polyQ) sequences of unknown normal function are present in a significant
number of proteins, and their repeat expansion is associated with a number of genetic …

The 17-residue N-terminus (httNT) directly flanking the polyQ sequence in huntingtin (htt) N-
terminal fragments plays a crucial role in initiating and accelerating the aggregation process …