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- W2891765626 abstract "The assembling of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor protein complex is a fundamental step in neuronal exocytosis, and it has been extensively studied in the last two decades. Yet, many details of this process remain inaccessible with the current experimental space and time resolution. Here, we study the zipping mechanism of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex computationally by using a coarse-grained model. We explore the different pathways available and analyze their dependence on the computational model employed. We reveal and characterize multiple intermediate states, in agreement with previous experimental findings. We use our model to analyze the influence of single-residue mutations on the thermodynamics of the folding process." @default.
- W2891765626 created "2018-09-27" @default.
- W2891765626 creator A5008561181 @default.
- W2891765626 creator A5046777747 @default.
- W2891765626 creator A5061903235 @default.
- W2891765626 creator A5081412017 @default.
- W2891765626 creator A5082744750 @default.
- W2891765626 date "2018-10-01" @default.
- W2891765626 modified "2023-09-26" @default.
- W2891765626 title "Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex" @default.
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- W2891765626 doi "https://doi.org/10.1016/j.bpj.2018.08.043" @default.