Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH.

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Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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Stepwise unfolding of human β2 ...... oidogenic precursor at low pH.

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Stepwise unfolding of human β2 ...... oidogenic precursor at low pH.

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Stepwise unfolding of human β2 ...... oidogenic precursor at low pH.

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Stepwise unfolding of human β2 ...... oidogenic precursor at low pH.

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Stepwise unfolding of human β2 ...... oidogenic precursor at low pH.

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Stepwise unfolding of human β2 ...... oidogenic precursor at low pH.

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P1476

Stepwise unfolding of human β2 ...... loidogenic precursor at low pH

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P2093

Anubhuti Singh

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Dominic Narang

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P2860

DE loop mutations affect beta2-microglobulin stability and amyloid aggregation

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The two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure

Three-dimensional structure of beta 2-microglobulin

Natively unfolded proteins: a point where biology waits for physics

The p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure.

Describing sequence-ensemble relationships for intrinsically disordered proteins.

Nucleated conformational conversion and the replication of conformational information by a prion determinant.

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe.

beta2-microglobulin-derived amyloidosis: an update.

P2888

s00249-016-1138-x

P304

65-76

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scholarly article

P356

10.1007/S00249-016-1138-X

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Samrat Mukhopadhyay

P577

2016-05-25T00:00:00Z

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P698

27225299

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