Modeling the interplay of glycine protonation and multiple histidine binding of copper in the prion protein octarepeat subdomains. (Q43433755)

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17 January 2020

title

Modeling the interplay of glycine protonation and multiple histidine binding of copper in the prion protein octarepeat subdomains (English)

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17 January 2020

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17 January 2020

Silvia Morante

3

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17 January 2020

Giancarlo Rossi

4

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17 January 2020

Giovanni La Penna

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17 January 2020

author name string

Francesco Guerrieri

1

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17 January 2020

Sara Furlan

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17 January 2020

publication date

2 December 2008

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Journal of Biological Inorganic Chemistry

17 January 2020

published in

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17 January 2020

volume

14

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17 January 2020

issue

3

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17 January 2020

page(s)

361-374

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Novel proteinaceous infectious particles cause scrapie

17 January 2020

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Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4.

21 January 2018

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Copper binding to the prion protein: structural implications of four identical cooperative binding sites

21 January 2018

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Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism

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XAFS study of the high-affinity copper-binding site of human PrP(91-231) and its low-resolution structure in solution

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Electron paramagnetic resonance evidence for binding of Cu(2 ) to the C-terminal domain of the murine prion protein

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Inter- and intra-octarepeat Cu(II) site geometries in the prion protein: implications in Cu(II) binding cooperativity and Cu(II)-mediated assemblies

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The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4.

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Soft self-consistent pseudopotentials in a generalized eigenvalue formalism

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Generalized Gradient Approximation Made Simple

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12 December 2020

Prion protein binds copper within the physiological concentration range

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Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides

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