Exploring Large Domain Motions in Proteins Using Atomistic Molecular Dynamics with Enhanced Conformational Sampling

Exploring Large Domain Motions in Proteins Using Atomistic Molecular Dynamics with Enhanced Conformational Sampling

Conformational transitions in multidomain proteins are essential for biological functions. The Apo conformations are typically open and flexible, while the Holo states form more compact conformations stabilized by protein-ligand interactions. Unfortunately, the atomically detailed mechanisms for suc...

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Bibliographic Details
Main Authors: Hisham M. Dokainish, Yuji Sugita
Format: Article
Language:English
Published: MDPI AG 2020-12-01
Series:International Journal of Molecular Sciences
Subjects:
molecular dynamics
enhanced conformational sampling algorithm
ribose binding protein
gREST_SSCR
free energy landscapes
hinge and twist angles
Online Access:https://www.mdpi.com/1422-0067/22/1/270

Internet

https://www.mdpi.com/1422-0067/22/1/270

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