CONFORMATIONAL ENERGY CALCULATIONS OF ENZYME‐SUBSTRATE INTERACTIONS. II. Computation of the Binding Energy for Substrates in the Active Site of α‐Chymotrypsin
- 1 May 1972
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 4 (3), 201-219
- https://doi.org/10.1111/j.1399-3011.1972.tb03420.x
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Determination of Intermolecular Potentials from Crystal Data. II. Crystal Packing with Applications to Poly(amino acids)Macromolecules, 1971
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1970
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1969
- Atomic CO-ordinates for tosyl-α-chymotrypsinBiochemical and Biophysical Research Communications, 1969
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1968
- Conformational Analysis of Macromolecules. IV. Helical Structures of Poly-L-Alanine, Poly-L-Valine, Poly-β-Methyl-L-Aspartate, Poly-γ-Methyl-L-Glutamate, and Poly-L-TyrosineThe Journal of Chemical Physics, 1967
- Re-evaluation of the Kinetic Constants of Previously Investigated Specific Substrates of α-Chymotrypsin1Journal of the American Chemical Society, 1955
- The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of Acetyl- and Nicotinyl-L-phenylalaninamide in Aqueous Solutions at 25° and pH 7.91Journal of the American Chemical Society, 1952
- The Kinetics of the α-Chymotrypsin Catalyzed Hydrolysis of Acetyl-L-tyrosinamide in Aqueous Solutions at 25° and pH 7.8-8.01Journal of the American Chemical Society, 1951
- The Kinetics of the α-Chymotrypsin Catalyzed Hydrolysis of Acetyl- and Nicotinyl-L-tryptophanamide in Aqueous Solutions at 25° and pH 7.91Journal of the American Chemical Society, 1951