Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

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 s...

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Veröffentlicht in:Biophysical journal 2018-10, Vol.115 (8), p.1470-1480
Hauptverfasser: Pinamonti, Giovanni, Campo, Gregory, Chen, Justin, Kluber, Alex, Clementi, Cecilia
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Proteins
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container_title Biophysical journal
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creator Pinamonti, Giovanni
Campo, Gregory
Chen, Justin
Kluber, Alex
Clementi, Cecilia
description 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.
doi_str_mv 10.1016/j.bpj.2018.08.043
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title Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex
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