Molecular dynamics simulations investigate the pathway of substrate entry active site of rhomboid protease
Author:
Affiliation:
1. Institute of Theoretical Chemistry, Jilin University, Changchun, China;
2. College of Chemistry and Biology, Beihua University, Jilin, China;
3. The Fungal Reference Laboratory of Shanghai Dermatology Hospital, Shanghai, China
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2018.1517609
Reference40 articles.
1. Essential dynamics of proteins
2. Architectural and thermodynamic principles underlying intramembrane protease function
3. Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate
4. Molecular dynamics with coupling to an external bath
5. Interaction Models for Water in Relation to Protein Hydration
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