June 27, 2007Proteins Structure Function and Bioinformatics
Protein conformational transitions explored by mixed elastic network models
Key result
A mixed elastic network model was developed to efficiently study large-scale conformational transitions of proteins, as demonstrated on KIF1A kinesin and myosin II.
Population
Motor proteins KIF1A kinesin and myosin II (computational models)
Design
Preclinical
Authors
Discussion
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Member takes
Implication
May advance motor protein modeling in cardiac research; leaves open experimental validation and clinical translation.
Structured PICO
P
Population
Motor proteins KIF1A kinesin and myosin II (computational models)
I
Intervention
Mixed elastic network model (MENM)
O
Outcome
Conformational transitions, transition paths, potentials of mean force, and partition functions
The developed mixed elastic network model provides a computationally efficient method to study large-scale conformational transitions in proteins like kinesin and myosin.
Cite This Study
Zheng et al. (2007) studied this question. Mixed elastic network model (MENM) was evaluated. A mixed elastic network model was developed to efficiently study large-scale conformational transitions of proteins, as demonstrated on KIF1A kinesin and myosin II.