Bacterial protease uses distinct thermodynamic signatures for substrate recognition.

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Bacterial protease uses distinct thermodynamic signatures for substrate recognition.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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Bacterial protease uses distinct thermodynamic signatures for substrate recognition.

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Bacterial protease uses distinct thermodynamic signatures for substrate recognition.

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Bacterial protease uses distinct thermodynamic signatures for substrate recognition.

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P1476

Bacterial protease uses distinct thermodynamic signatures for substrate recognition

@en

P2093

Adam Round

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Guillaume Hoffmann

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Irina Cornaciu

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José A Márquez

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Sofiya Fedosyuk

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Takayuki K Nemoto

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Yuko Ohara-Nemoto

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P2860

Electrostatics of nanosystems: application to microtubules and the ribosome

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Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III

Ligand binding stepwise disrupts water network in thrombin: enthalpic and entropic changes reveal classical hydrophobic effect

S46 Peptidases are the First Exopeptidases to be Members of Clan PA

XDS

Coot: model-building tools for molecular graphics

P2888

s41598-017-03220-y

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2848

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P31

scholarly article

P356

10.1038/S41598-017-03220-Y

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P407

English

P433

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P478

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P50

Kristina Djinovic-Carugo

Gustavo A Bezerra

P577

2017-06-06T00:00:00Z

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P6179

1085782835

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P698

28588213

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P932

5460201

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