Muhammad H. Zaman1
Molecular & Cellular Biomechanics, Vol.2, No.4, pp. 179-190, 2005, DOI:10.3970/mcb.2005.002.179
Abstract We report the results of longest to date simulation on misfolding of monomeric human prion protein (HuPrP). By comparing our simulation of a partially unfolded protein to the simulation of the native protein, we observe that the native protein as well as native regions in the partially unfolded protein remain in the native state, and the unfolded regions fold back with increased extended (sheet and PP-II) conformations. The misfolded regions show increased basin hopping from non-helical basins while the amino acids locked in the helical conformation tend to stay locked in that conformation. Our results More >
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