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Thursday, August 27, 2009

FEBS Letters Special Issue on Protein Folding, Misfolding and Disease

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FEBS Letters Special Issue

Volume 583, Issue 16, Pages 2579-2700 (20 August 2009)
Protein Folding, Misfolding and Disease

Edited by Per Hammarström and Peter Brzezinski

Protein aggregation was for decades regarded as a mere nuisance in protein research. This process often occurred after a tedious isolation procedure for functional studies and in concentrated protein solutions used for setting up crystallization screens. Just as frustrating were the early days of protein folding. Scientists were equally frustrated in detecting a turbid sample in the dialysis bag when returning to the lab in the early morning hours as to find that their refolded protein sample lacked specific activity or turned opalescent during rapid dilution of a chemically denatured protein in the stopped flow machine or during thermal denaturation. Few researchers at the time realized that the misfolded states of proteins would hold the key to some of the most severely debilitating diseases known to man.

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Issue 16 /2009
FEBS Letters Special Issue: Protein Folding, Misfolding and Disease

Managing Editor
Felix Wieland
Heidelberg University,
Heidelberg, Germany
Email: felix.wieland@bzh.
uni-heidelberg.de

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