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• W2076675152 abstract "The overall motions and atomic fluctuations of DHFR are calculated using molecular dynamics simulations to explore potential links between catalysis and dynamics in this enzyme system. Calculations of 10 ns duration were performed on three ternary complexes from the DHFR catalytic cycle:  DHFR/DHF/NADPH (DH), DHFR/THF/NADP+ (TP), and DHFR/THF/NADPH (TH). The protein maintains a core structure very similar to the initial X-ray model, while several flexible loops undergo conformational changes. Comparison of the dynamics of the protein in the different complexes demonstrates that the ligands affect the behavior of the protein even though the ligands only differ by one to two hydrogen atoms. In particular, strong-coupled motions that appear in the reactive complex DH disappear in the product complexes, indicating that these motions may be linked to catalysis. Furthermore, mutants, which have been observed to be debilitating to particular chemical steps in catalysis, occur with high correlation in the regions..." @default.
• W2076675152 created "2016-06-24" @default.
• W2076675152 creator A5060440052 @default.
• W2076675152 creator A5091723370 @default.
• W2076675152 date "1999-12-28" @default.
• W2076675152 modified "2023-09-27" @default.
• W2076675152 title "Protein Dynamics in Enzymatic Catalysis: Exploration of Dihydrofolate Reductase" @default.
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• W2076675152 doi "https://doi.org/10.1021/ja9913838" @default.
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