Preliminary attempt to follow the enthalpy of an enzymatic reaction by ab initio computations: Catalytic action of papain
- 1 December 1978
- journal article
- Published by Wiley in International Journal of Quantum Chemistry
- Vol. 14 (6), 815-838
- https://doi.org/10.1002/qua.560140613
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Analytical potentials from "ab initio" computations for the interaction between biomolecules. 1. Water with amino acidsJournal of the American Chemical Society, 1977
- Ab initio molecular orbital studies on the active site of papainChemical Physics Letters, 1976
- Binding of chloromethyl ketone substrate analogs to crystalline papainBiochemistry, 1976
- Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acidsThe Journal of Physical Chemistry, 1975
- Energy functions for peptides and proteins. I. Derivation of a consistent force field including the hydrogen bond from amide crystalsJournal of the American Chemical Society, 1974
- Non‐bonded interatomic potential functions and crystal structure. Correction of the functions for use with macromolecules and application to polypeptide helixesPeptide Science, 1973
- A real-space refinement procedure for proteinsActa Crystallographica Section A, 1971
- On NH···S hydrogen bondsJournal of Molecular Biology, 1969
- Study of the electronic structure of molecules. XI. Comments on some present aspects and tentative extrapolationsInternational Journal of Quantum Chemistry, 1969
- Structure of PapainNature, 1968