Abstract
AbstractCalculating the electrostatic potential around the Ser–His–Asp catalytic triad in serine proteinases the very important substituent effect of the buried aspartate is revealed. It is found that the strong Coulomb field of this distant but charged side chain considerably enhances the nucleophilicity of the active serine hydroxyl group. The interpretation of the vital importance of aspartate may replace the “charge–relay” hypothesis which seems to be disproved in the light of recent experiments.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
