Hello everyone I just solved a structure of a catalytic protein with very long water chains (35 to 40 continuous water molecules) recently and found that the catalytic bed is with less polarity (compared to other orthologues) using computaional methods. I believe that these can help in ligand accesibility as the enzyme has decreased ligand binding exposed surface, compared to other orthologues. Since the pH of the crystallization condition is 5.6, how can I distinguish if the water chains are from acidic condition or are present to imoprove polarity thereby increasing ligand accessibility? I will be very much grateful for your help and kind responses.
Cheers Dr. Rakesh Chatterjee Project Scientist II Dr Neelagandan Kamariah Lab CCBT, BRIC inStem, GKVK campus, Bellary Road, Bangalore, India-560065 ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
