Journal
FEBS LETTERS
Volume 513, Issue 2-3, Pages 267-272Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02335-9
Keywords
aggregation; glutathione S-transferase; Huntington; polyglutamine; structure
Ask authors/readers for more resources
Aggregation of expanded polyglutamine (polyQ) seems to be the cause of various genetic neuro degenerative 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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available