Molecular dynamics simulations of wild-type and point mutation human prion protein at normal and elevated temperature

E  El-Bastawissy; M H  Knaggs; I H  Gilbert

doi:10.1016/S1093-3263(01)00113-9

Molecular dynamics simulations of wild-type and point mutation human prion protein at normal and elevated temperature

E El-Bastawissy
, M H Knaggs
, I H Gilbert

Research output: Contribution to journal › Article › peer-review

53 Citations (Scopus)

Abstract

This paper describes molecular dynamics simulations of prion protein at 300 and 500 K. This was undertaken to gain insight into the factors involved in the stability of prion protein. Simulations were done using the Particle Mesh Ewald (PME) method using a homology model of the C-terminal fragment of human prion protein and the NMR structure of the human prion protein. The simulations at both 300 and 500 K were stable. Simulations were also undertaken with a mutant known to be associated with prion disease: Asp178Asn. The Asp178Asn simulation trajectory was observed to be much less stable than for the wild-type protein trajectory. Significant breakdown in secondary structure was observed for Asp178Asn at 500 K. (C) 2001 Elsevier Science Inc. All rights reserved.

Original language	English
Pages (from-to)	145-154
Number of pages	10
Journal	Journal of Molecular Graphics and Modelling
Volume	20
Issue number	2
DOIs	https://doi.org/10.1016/S1093-3263(01)00113-9
Publication status	Published - 2001

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10.1016/S1093-3263(01)00113-9

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title = "Molecular dynamics simulations of wild-type and point mutation human prion protein at normal and elevated temperature",

abstract = "This paper describes molecular dynamics simulations of prion protein at 300 and 500 K. This was undertaken to gain insight into the factors involved in the stability of prion protein. Simulations were done using the Particle Mesh Ewald (PME) method using a homology model of the C-terminal fragment of human prion protein and the NMR structure of the human prion protein. The simulations at both 300 and 500 K were stable. Simulations were also undertaken with a mutant known to be associated with prion disease: Asp178Asn. The Asp178Asn simulation trajectory was observed to be much less stable than for the wild-type protein trajectory. Significant breakdown in secondary structure was observed for Asp178Asn at 500 K. (C) 2001 Elsevier Science Inc. All rights reserved.",

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AU - Knaggs, M H

AU - Gilbert, I H

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Y1 - 2001

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AB - This paper describes molecular dynamics simulations of prion protein at 300 and 500 K. This was undertaken to gain insight into the factors involved in the stability of prion protein. Simulations were done using the Particle Mesh Ewald (PME) method using a homology model of the C-terminal fragment of human prion protein and the NMR structure of the human prion protein. The simulations at both 300 and 500 K were stable. Simulations were also undertaken with a mutant known to be associated with prion disease: Asp178Asn. The Asp178Asn simulation trajectory was observed to be much less stable than for the wild-type protein trajectory. Significant breakdown in secondary structure was observed for Asp178Asn at 500 K. (C) 2001 Elsevier Science Inc. All rights reserved.

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JO - Journal of Molecular Graphics and Modelling

JF - Journal of Molecular Graphics and Modelling

IS - 2

ER -

Molecular dynamics simulations of wild-type and point mutation human prion protein at normal and elevated temperature

Abstract

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