How Robust Is the Mechanism of Folding-Upon-Binding for an Intrinsically Disordered Protein?

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How Robust Is the Mechanism of Folding-Upon-Binding for an Intrinsically Disordered Protein?

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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How Robust Is the Mechanism of ...... rinsically Disordered Protein?

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How Robust Is the Mechanism of ...... rinsically Disordered Protein?

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Item

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How Robust Is the Mechanism of ...... rinsically Disordered Protein?

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How Robust Is the Mechanism of ...... rinsically Disordered Protein?

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How Robust Is the Mechanism of ...... rinsically Disordered Protein?

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How Robust Is the Mechanism of ...... rinsically Disordered Protein?

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P1476

How Robust Is the Mechanism of ...... rinsically Disordered Protein?

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P2093

Daniela Bonetti

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Francesca Troilo

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Maurizio Brunori

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Sonia Longhi

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Stefano Gianni

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P2860

Intrinsically unstructured proteins and their functions

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The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

Natively unfolded proteins: a point where biology waits for physics

Understanding protein non-folding.

Structural basis for the attachment of a paramyxoviral polymerase to its template.

Kinetics of folding and binding of an intrinsically disordered protein: the inhibitor of yeast aspartic proteinase YPrA.

Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.

Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants

P304

1889-1894

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scholarly article

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10.1016/J.BPJ.2018.03.017

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English

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P478

114

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P577

2018-04-01T00:00:00Z

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29694866

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P932

5937165

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