Published September 1978
| Published
Book Section - Chapter
Open
A Study by Nitrogen-15 Nuclear Magnetic Resonance Spectroscopy of the State of Histidine in the Catalytic Triad of α-Lytic Protease
- Creators
- Bachovchin, William W.
- Roberts, John D.
Chicago
An error occurred while generating the citation.
Abstract
Hydrolytic cleavage of peptide bonds is an energetically· favorable reaction, but one that normally takes place very slowly at room temperature, even in the presence of rather strong acids or bases. It can be strongly catalyzed by many proteases, and much effort has been expended to determine how these have the ability to increase the rate of hydrolysis by a million-fold or more in neutral solutions. One of the types of proteases, the serine-protease family, is characterized by the presence at the active site of a "catalytic triad" comprised of the side-chain residues of serine, histidine and aspartic acid.
Additional Information
© 1978 International Union of Pure and Applied Chemistry. Supported by the Public Health Service, Research Grant No. GM-11072 from the Division of General Medical Sciences, and by the National Science Foundation. We are greatly indebted to Professor John H. Richards and Dr. Michael W. Hunkapiller for their unfailing interest and assistance throughout the course of this research, but we should emphasize that they are in no way responsible for its deficiencies either in the experiments or our interpretation of the results.Attached Files
Published - 404419.pdf
Files
404419.pdf
Files
(419.3 kB)
| Name | Size | Download all |
|---|---|---|
|
md5:ccde49ccb7db5c19a6447ffa3938a2b2
|
419.3 kB | Preview Download |
Additional details
- Eprint ID
- 61714
- Resolver ID
- CaltechAUTHORS:20151029-115032732
- U.S. Public Health Service (USPHS)
- GM-11072
- NSF
- Created
-
2015-11-04Created from EPrint's datestamp field
- Updated
-
2019-10-03Created from EPrint's last_modified field