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The Protein Folding Network
Author(s):
Francesco Rao, Amedeo Caflisch
Institution:
Computational Structural Biology Group - Department of Biochemistry - University of Zurich
Year:
2004
URL:
http://www.biochem-caflisch.unizh.ch/ruvido/protein_folding_network.htm
Project Description:
The energy landscape for the folding of the beta3s peptide is investigated by Molecular Dynamics simulations. Conformations of the peptide and the transitions between them are the nodes and the links of the network, respectively. The size and color coding of the nodes reflect the statistical weight and average neighbor connectivity. Representative conformations are shown by a pipe colored according to secondary structure: white stands for coil, red for alpha-helix, orange for bend, cyan for strand and the N-terminus is in blue. The variable radius of the pipe reflects structural variability within snapshots in a conformation. The yellow diamonds are folding TS conformations.

Source: F. Rao and A. Caflisch, JMB 342, 299-306 (2004)

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