Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsin-Reference-Cited by-同舟云学术

Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsin

Published:1981-10 Issue:22 Volume:20 Page:6462-6474
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kossiakoff Anthony A.,Spencer Steven A.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00525a027

Reference86 articles.

1. A hydrogen-bond network at the active site of subtilisin BPN'

2. Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases

3. Bacon, G. E. (1975) in Neutron Diffraction, p39, Clarendon Press, Oxford.

4. The Current Status of the α-Chymotrypsin Mechanism

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