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- W2896183810 abstract "Proteins constantly interact and often form molecular complexes. The dynamics of most biological processes strongly rely on the kinetics and thermodynamics of assembly and disassembly of these complexes. Consequently an accurate characterization of these kinetics and thermodynamics that underlie them provides key information to better understand these processes. Here, we present two efficient techniques to quantify the assembly and disassembly of protein complexes: isothermal titration calorimetry and fluorescence anisotropy. As an example we focus on the formation of SNAREpins and also present how to prepare SNARE proteins to use in these experimental setups. We then show how to use these techniques to determine the critical factors that activate assembly kinetics." @default.
- W2896183810 created "2018-10-26" @default.
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- W2896183810 date "2018-10-14" @default.
- W2896183810 modified "2023-10-15" @default.
- W2896183810 title "SNAREpin Assembly: Kinetic and Thermodynamic Approaches" @default.
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- W2896183810 doi "https://doi.org/10.1007/978-1-4939-8760-3_5" @default.
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