W
W. Andrzej Sokalski
Researcher at Wrocław University of Technology
Publications - 77
Citations - 2339
W. Andrzej Sokalski is an academic researcher from Wrocław University of Technology. The author has contributed to research in topics: Ab initio & Active site. The author has an hindex of 26, co-authored 77 publications receiving 2244 citations. Previous affiliations of W. Andrzej Sokalski include Jackson State University & Johns Hopkins University.
Papers
More filters
Journal ArticleDOI
Cumulative atomic multipole representation of the molecular charge distribution and its basis set dependence
TL;DR: A simple procedure to decompose the theoretical molecular charge distribution into cumulative atomic multipoles supplementing any population analysis scheme has been described and tested for a number of molecules in extended basis sets as mentioned in this paper.
Journal ArticleDOI
An efficient procedure for decomposition of the scf interaction energy into components with reduced basis set dependence
TL;DR: In this article, the basis set dependence of the exchange term in He 2, (LiH) 2 and Li + …H 2 O has been considerably reduced, matching exchange perturbation results and avoiding artificial attractive values appearing in other procedures of this kind.
Journal ArticleDOI
How short can the H...H intermolecular contact be? New findings that reveal the covalent nature of extremely strong interactions.
TL;DR: An analysis of the interaction energy components for dihydrogen bonded systems considered indicates that in contrast to conventional hydrogen bonded systems the attractive electrostatic term is outweighed by the repulsive exchange energy term and that the higher order delocalization energy term is the most important attractive term.
Journal ArticleDOI
Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction.
Kara E. Ranaghan,Lars Ridder,Borys Szefczyk,W. Andrzej Sokalski,Johannes C. Hermann,Adrian J. Mulholland +5 more
TL;DR: Transition state stabilization (by electrostatic interactions, including hydrogen bonds) is found to be central to catalysis by the enzyme, with contributions from residues Arg90, Arg7, and Arg63.
Journal ArticleDOI
Differential transition-state stabilization in enzyme catalysis: quantum chemical analysis of interactions in the chorismate mutase reaction and prediction of the optimal catalytic field.
TL;DR: Comparison with the active site of the enzyme from those of several species shows that the positions of charged active site residues correspond closely to the optimal catalytic field, showing that the enzyme has evolved specifically to stabilize the TS relative to the substrate.