The prion-like folding behavior in aggregated proteins

Details The prion-like folding behavior in aggregated proteins The prion-like folding behavior in aggregated proteins

2005-06-09

arxiv.org/abs/q-bio/0506012v1

Physical Review E 72, 041912 (2005), Virtual Journal of Biological Physics Research(October 15, 2005)

Biology

Quantitative Biology

Biomolecules

7 pages, 6 figures

Scientific paper

10.1103/PhysRevE.72.041912

We investigate the folding behavior of protein sequences by numerically studying all sequences with maximally compact lattice model through exhaustive enumeration. We get the prion-like behavior of protein folding. Individual proteins remaining stable in the isolated native state may change their conformations when they aggregate. We observe the folding properties as the interfacial interaction strength changes, and find that the strength must be strong enough before the propagation of the most stable structures happens.

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