Maybe you would also be interested in http://www.jinkai.org/AAD_history.html
Regards, Kevin On Tue, Feb 7, 2012 at 8:52 AM, Christian Roth <christian.r...@bbz.uni-leipzig.de> wrote: > Hi, > > you may also look into the papers of John A. Gerlt, who did a lot on > protonabtraction reactions and the theory behind this. Esspecially the pKa > disturbance and the match to the pkA of the substrate of the reaction. > > Best Wishes > > Christian > > Am Dienstag 07 Februar 2012 12:48:26 schrieb Deepak Oswal: >> Dear colleagues, >> >> We have solved the crystal structure of a human enzyme. The pKa of a >> catalytically critical aspartic acid has increased to 6.44. It is hydrogen >> bonded (2.8 Angstroms) to a water molecule that is supposed to donate a >> proton during the catalysis. Can anybody help me a) interpret the >> significance of this increase in pKa of the aspartic acid from 3.8 to 6.44 >> in context with the catalysis? Is this advantageous or detrimental? b) How >> is pKa related to an amino acids’ ability to force a water molecule to >> donate a proton? c) At pH 7.4, the aspartic acid would be de-protonated >> irrespective of whether the pKa is 3.8 or 6.44; isn’t that true? d) Have >> similar increase in pKa values observed for aspartic acids before? I would >> be grateful if anybody could explain or comment on the above queries. >> >> Deepak Oswal >>
