Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.

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P2860

Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

@ast

Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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P1476

Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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P2093

Daiqian Xie

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

Yanzi Zhou

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

Yingkai Zhang

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

P2860

A clogged gutter mechanism for protease inhibitors.

Rigidification of a Flexible Protease Inhibitor Variant upon Binding to Trypsin

Functional and Structural Roles of the Cys14–Cys38 Disulfide of Bovine Pancreatic Trypsin Inhibitor

Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis

Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex

Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen A alpha: geometry of the catalytic triad and interactions of the P1', P2', and P3' substrate residues

Comparison of multiple Amber force fields and development of improved protein backbone parameters

Protein inhibitors of proteinases

The role of the protein core in the inhibitory power of the classic serine protease inhibitor, chymotrypsin inhibitor 2.

What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?

P304

1138-1142

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scholarly article

P356

10.1021/ACS.JPCLETT.6B00373

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P478

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2016-03-09T00:00:00Z

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26958702

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P921

proteolysis

P932

4824663

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Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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P2860

P2860

Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P932