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Titlebook: Specificity in Biological Interactions; Proceedings of a Wor C. Chagas,B. Pullman Conference proceedings 1984 Pontificia Academia Scientiar

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11#
發(fā)表于 2025-3-23 11:31:33 | 只看該作者
12#
發(fā)表于 2025-3-23 14:50:32 | 只看該作者
Simulating the Energetics and Dynamics of Enzymatic Reactionsthe relationship between reaction free energies (ΔG.) and activation free energies (Δg≠) in enzyme catalysis. The preliminary results presented here indicate that the rates of proton transfer reactions in enzymes might be correlated in a simple way with the corresponding pK. differences.
13#
發(fā)表于 2025-3-23 21:05:19 | 只看該作者
14#
發(fā)表于 2025-3-23 22:42:02 | 只看該作者
15#
發(fā)表于 2025-3-24 03:06:45 | 只看該作者
Theoretical Analysis of Factors Responsible for Specificity in Ionophore-Cation InteractionsK., NH.+ with nonactin and Mg., Ca. with ionophore A 23187. The delimitation in each case of the different components of the interaction energy and the inclusion of the solvation-desolvation aspects of the interaction enable to account for the selectivity and specificity observed in each of these associations.
16#
發(fā)表于 2025-3-24 09:16:05 | 只看該作者
17#
發(fā)表于 2025-3-24 12:39:47 | 只看該作者
Theoretical Studies of Molecular Recognition and Catalysis by Enzymesity of the potential functions and methodology used in the computations, and demonstrates the utility of this methodology in providing an understanding of the interactions that lead to molecular recognition.
18#
發(fā)表于 2025-3-24 18:19:04 | 只看該作者
19#
發(fā)表于 2025-3-24 20:51:15 | 只看該作者
Elements of Specific Recognition of Non-Intercalating Ligands in the Interaction with DNAon- intercalators..It is documented that base pair specificity, groove binding and geometrical requirements of their interaction are related to the properties inherent in the structure and dynamics of both the interacting ligand and nucleic acid.
20#
發(fā)表于 2025-3-25 03:03:46 | 只看該作者
Structural Studies of DNA-Protein Interactionsgulate gene expression. DNA-protein recognition appears to be based primarily on a network of hydrogen bonds between side-chains of the protein and the parts of the base-pairs exposed within the major groove of the DNA.
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