(Q44306002)

English

Optimized overproduction, purification, characterization and high-pressure sensitivity of the prion protein in the native (PrP(C)-like) or amyloid (PrP(Sc)-like) conformation.

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18 December 2019

Optimized overproduction, purification, characterization and high-pressure sensitivity of the prion protein in the native (PrP(C)-like) or amyloid (PrP(Sc)-like) conformation (English)

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18 December 2019

prion protein family

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18 December 2019

Jean-Michel Verdier

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18 December 2019

author name string

Maria Teresa Alvarez-Martinez

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18 December 2019

Reinhard Lange

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18 December 2019

Claude Balny

5

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18 December 2019

Jean-Pierre Liautard

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18 December 2019

publication date

1 February 2003

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18 December 2019

Biochimica et Biophysica Acta

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18 December 2019

1645

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18 December 2019

2

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18 December 2019

228-240

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18 December 2019

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Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy

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pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231)

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Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein.

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Physical studies of conformational plasticity in a recombinant prion protein

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Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates

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Kinetic intermediate in the folding of human prion protein

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The role of disulfide bridge in the folding and stability of the recombinant human prion protein

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Analytical background and discussion of the chaperone model of prion diseases

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Pressure provides new insights into protein folding, dynamics and structure

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Identifiers

10.1016/S1570-9639(02)00536-8

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18 December 2019

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18 December 2019

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