Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/99170
Title: The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions : a replica exchange molecular dynamics study
Authors: Zhang, John Z. H.
Lu, Xiaoliang
Zeng, Juan
Gao, Ya
Zhang, Dawei
Mei, Ye
Issue Date: 2013
Source: Lu, X., Zeng, J., Gao, Y., Zhang, J. Z. H., Zhang, D., & Mei, Y. (2013). The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions: a replica exchange molecular dynamics study. Journal of Molecular Modeling, 19(11), 4897-4908.
Series/Report no.: Journal of molecular modeling
Abstract: Replica exchange molecular dynamics simulations in neutral and acidic aqueous solutions were employed to study the intrinsic helical propensities of three helices in both Syrian hamster (syPrP) and human (huPrP) prion proteins. The helical propensities of syPrP HA and huPrP HA are very high under both pH conditions, which implies that HA is barely involved in the helix-to-β transition. The SyPrP HB chain has a strong tendency to adopt an extended conformation, which is possibly involved in the mechanism of infectious prion diseases in Syrian hamster. HuPrP HC has more of a preference for the extended conformation than huPrP HA and huPrP HB do, which leads to the conjecture that it is more likely to be the source of β-rich structure for human prion protein. We also noticed that the presence of salt bridges is not correlated with helical propensity, indicating that salt bridges do not stabilize helices.
URI: https://hdl.handle.net/10356/99170
http://hdl.handle.net/10220/17372
DOI: http://dx.doi.org/10.1007/s00894-013-1985-7
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SPMS Journal Articles

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