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. 2012 Mar 19;7(3):e32075. doi: 10.1371/journal.pone.0032075

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Fritsche et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Inline graphic — The energy of a residue is its interaction energy with neighboring residues within the range of interaction. The magnitude of the repulsive and the attractive energy and their differences in consecutive segments increases with temperature which is manifested in the global (coil-to-globule) structure of the protein. At low temperatures (), residues with the lowest mobility consist of 36R, 37K, 57E, 62E, 65E, 72R, 73D, 75K, 76K, 78R, 89R, 90N, 91D, 92E, 93E, 95N, 96K, 119K, 120K, 134K, 135K, 141Q and 142E. Nearly all the electrostatic residues (D, E, K, R) along with a few polar groups (Q,N) act as anchor/seed for segmental aggregation.

Inline graphic — The energy of a residue is its interaction energy with neighboring residues within the range of interaction. The magnitude of the repulsive and the attractive energy and their differences in consecutive segments increases with temperature which is manifested in the global (coil-to-globule) structure of the protein. At low temperatures (), residues with the lowest mobility consist of 36R, 37K, 57E, 62E, 65E, 72R, 73D, 75K, 76K, 78R, 89R, 90N, 91D, 92E, 93E, 95N, 96K, 119K, 120K, 134K, 135K, 141Q and 142E. Nearly all the electrostatic residues (D, E, K, R) along with a few polar groups (Q,N) act as anchor/seed for segmental aggregation.