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Journal/Book: Folding and Design
Published: 1996
Pages: R95 - R106
Volume: 1
Issue: 5
Accession no.: 23
ISBN: 1359-0278

The concept of a random coil: Residual structure in peptides and denatured proteins

Lorna J Smith, Klaus M Fiebig, Harald Schwalbe, Christopher M Dobson
Non-native states of proteins are of increasing interest because of their relevance to issues such as protein folding, translocation and stability. A framework for interpreting the wealth of experimental data for non-native states emerging from rapid advances in experimental techniques involves comparison with a [`]random coil' state, which possesses no structure except that inherent in the local interactions. We review here the concept of a random coil, from its global to its local properties. In particular, we focus on the description of a random coil in terms of statistical distributions in [phi], [psi] space. We show that such a model, in combination with experimental data, provides insight into the structural properties of polypeptide chains and has significance for understanding protein folding and for molecular design.
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Prof. Dr. Harald Schwalbe
Institut für Organische Chemie und Chemische Biologie
Johann Wolfgang Goethe Universität
Max-von-Laue-Str. 7
D-60438 Frankfurt am Main
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