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Updated: Jun 27, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
08:49

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

アルファベータ並列タンパク質の折りたたむ過程で, (非) 本来の構造要素が展開された分子にドッキングしたため,経路外の種が広範囲に形成される

Sanne M Nabuurs1, Adrie H Westphal, Carlo P M van Mierlo

  • 1Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands.

Journal of the American Chemical Society
|December 5, 2008
PubMed
まとめ

タンパク質の展開は,アポフラボドキシンにおける一時的な螺旋構造を明らかにする. 展開状態のこれらの非本来の相互作用は,予期せぬ形で経路外折り合いを促進し,効率的なタンパク質折り合いを妨げます.

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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

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