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Solution structure of polyglutamine tracts in GST‐polyglutamine fusion proteins
Author(s) -
Masino Laura,
Kelly Geoff,
Leonard Kevin,
Trottier Yvon,
Pastore Annalisa
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02335-9
Subject(s) - context (archaeology) , protein aggregation , fusion protein , random coil , biophysics , fusion , chemistry , biochemistry , biology , microbiology and biotechnology , circular dichroism , gene , recombinant dna , paleontology , linguistics , philosophy
Aggregation of expanded polyglutamine (polyQ) seems to be the cause of various genetic neurodegenerative diseases. Relatively little is known as yet about the polyQ structure and the mechanism that induces aggregation. We have characterised the solution structure of polyQ in a proteic context using a model system based on glutathione S ‐transferase fusion proteins. A wide range of biophysical techniques was applied. For the first time, nuclear magnetic resonance was used to observe directly and selectively the conformation of polyQ in the pathological range. We demonstrate that, in solution, polyQs are in a random coil conformation. However, under destabilising conditions, their aggregation behaviour is determined by the polyQ length.