Nonempirical analysis of nature of catalytic effects in ribonuclease A active site

✍ Scribed by K??dzierski, Pawe?; Sokalski, W. Andrzej; Krauss, Morris

• Book ID: 101221796
• Publisher: John Wiley and Sons
• Year: 2000
• Tongue: English
• Weight: 405 KB
• Volume: 21
• Category: Article
• ISSN: 0192-8651
• DOI: 10.1002/(sici)1096-987x(20000430)21:6<432::aid-jcc3>3.0.co;2-7

✦ Synopsis

The physical nature of the catalytic activity exerted by various ribonuclease A active site constituents is analyzed in terms of the differential transition state stabilization approach in which activation barrier changes induced by the molecular environment are expressed by additive components defined in the theory of intermolecular interactions. Electrostatic multipole contributions seem to approximate total catalytic activity well for residues separated by contacts longer than 2.7 Å whereas at shorter distances the remaining exchange and delocalization terms are not negligible. Depending on the reaction step, the same residue may exhibit catalytic or inhibitory activity.