High Pressure Studies on Transthyretin

Author: Foguel, Debora

Source: Protein and Peptide Letters, Volume 12, Number 3, April 2005 , pp. 245-249(5)

Publisher: Bentham Science Publishers

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Abstract:

High hydrostatic pressure (HHP) is a powerful tool to study protein folding and the dynamics and structure of folding intermediates. Aggregates and amyloids, derived from partially folding intermediates at the junction between productive and off-pathway folding, have been studied as well, which promises better understanding of the protein misfolding diseases. Here is summarized the recent data we have collected with transthyretin under pressure.

Keywords: amyloidogenic diseases; high hydrostatic pressure; protein aggregation; protein folding; transthyretin

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866053587200

Affiliations: Departamento de Bioquimica Medica, Programa de Biologia estrutural, Instituto de Ciencias Biomedicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, 21941-590, Brazil.

Publication date: April 1, 2005

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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