The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action (Q27666029)

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English	The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action	scientific article

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16 January 2020

The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action (English)

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16 January 2020

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16 January 2020

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16 January 2020

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Weixiao Yuan Wahlgren

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16 January 2020

Pálma Porrogi

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16 January 2020

Borbála Szenthe

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16 January 2020

András Patthy

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16 January 2020

László Gráf

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16 January 2020

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21 November 2010

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16 January 2020

Journal of Biological Chemistry

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16 January 2020

286

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16 January 2020

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16 January 2020

3587-3596

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16 January 2020

Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction

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Structure of a serine protease poised to resynthesize a peptide bond

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The determination of protonation states in proteins

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Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis

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X-ray structure of a serine protease acyl-enzyme complex at 0.95-A resolution

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A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment

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A low-barrier hydrogen bond in the catalytic triad of serine proteases

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20 March 2017

Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin

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How do serine proteases really work?

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Serine Proteases: Structure and Mechanism of Catalysis

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When the surface tells what lies beneath: combinatorial phage-display mutagenesis reveals complex networks of surface-core interactions in the pacifastin protease inhibitor family.

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Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins

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High resolution nuclear magnetic resonance study of the histidine—Aspartate hydrogen bond in chymotrypsin and chymotrypsinogen

1 reference

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10.1074/JBC.M110.161604

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16 January 2020

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16 January 2020

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16 January 2020

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