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Surface Electrostatic Charge Distributions

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Molecular Structures and Structural Dynamics of Prion Proteins and Prions

Part of the book series: Focus on Structural Biology ((FOSB,volume 9))

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Abstract

In Chaps. 2 ∼ 5, we found rabbit prion protein has a structural conformational change from α-helices into β-sheets at 350 and 450 K in the environments from neutral pH to low pH. However, the resistant species dogs and horses , and the nonresistant species humans and mice do not have such performance. Thus, we may say that SBs (such as D177-R163 , the ‘bow string’ of the S2-H2 loop) clearly contribute to the structural stability of rabbit prion protein. The nonresistant species humans and mice do not always have this ‘bow string’. This provides a clue of treatments of prion diseases. Clearly, there should be many other clues (for example, surface electrostatic charge distributions (Sect. 9.2), copper binding (Sect. 9.3.1) to reveal the secret of rabbits resisting to prion diseases.

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Authors and Affiliations

  1. School of Sciences Information Technology and Engineering, The Federation University, Ballarat, VIC, Australia

    Jiapu Zhang

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  1. Jiapu Zhang
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Zhang, J. (2015). Surface Electrostatic Charge Distributions. In: Molecular Structures and Structural Dynamics of Prion Proteins and Prions. Focus on Structural Biology, vol 9. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-7318-8_9

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