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Proceedings of the National Academy of Sciences of the United States of America|February 19, 2000
Low dielectric response in enzyme active siteE L Mertz, L I KrishtalikMolekuliarnaia Biologiia|July 1, 1984
[Intraglobular electrostatic field of an enzyme. IV. Electrolytic dissociation of the active center of alpha-chymotrypsin]L I Krishtalik, V V TopolevMolekuliarnaia Biologiia|September 1, 1983
[The intraglobular electrostatic field of an enzyme. 1. The primary field created by the polypeptide core, functional groups and ions of the alpha-chymotrypsin molecule]L I Krishtalik, V V TopolevBiochimica Et Biophysica Acta|August 5, 2000
Effects of medium polarization and pre-existing field on activation energy of enzymatic charge-transfer reactionsL I Krishtalik, V V TopolevMolekuliarnaia Biologiia|May 1, 1984
[Intraglobular electrostatic field of an enzyme. Calculation of the dissociation constant of a protein ionogenic group. Dissociation of Asp-102 chymotrypsin]L I Krishtalik, V V TopolevBioelectrochemistry and Bioenergetics (Lausanne, Switzerland)|June 24, 1999
Free energy of charge transfer and intraprotein electric field: method of calculation depends on the charge state of protein at a given structureE L Mertz, L I KrishtalikFEBS Letters|August 7, 1995
On the physical basis for the cis-positive rule describing protein orientation in biological membranesL I Krishtalik, W A CramerMolekuliarnaia Biologiia|November 1, 1983
[The intraglobular electrostatic field of an enzyme. II. Effect of environment polarization]V V Topolev, L I KrishtalikProteins|June 1, 1997
Electrostatics of proteins: description in terms of two dielectric constants simultaneouslyL I Krishtalik, A M Kuznetsov, E L MertzPageof 3