期刊
MOLECULAR PHYSICS
卷 116, 期 21-22, 页码 3173-3180出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/00268976.2018.1496290
关键词
Molten globule; lattice model; protein folding; multi-state folders; heat capacity
资金
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek [722.011.009]
The majority of proteins perform their cellular function after folding into a specific and stable native structure. Additionally, for many proteins less compact molten globule' states have been observed. Current experimental observations show that the molten globule state can show varying degrees of compactness and solvent accessibility; the underlying molecular cause for this variation is not well understood. While the specificity of protein folding can be studied using protein lattice models, current design procedures for these models tend to generate sequences without molten globule-like behaviour. Here we alter the design process so the distance between the molten globule ensemble and the native structure can be steered; this allows us to design protein sequences with a wide range of folding pathways, and sequences with well-defined heat-induced molten globules. Simulating these sequences we find that (1) molten globule states are compact, but have less specific configurations compared to the folded state, (2) the nature of the molten globule state is highly sequence dependent, (3) both two-state and multi-state folding proteins may show heat-induced molten globule states, as observed in heat capacity curves. The varying nature of the molten globules and typical heat capacity curves associated with the transitions closely resemble experimental observations. [GRAPHICS] .
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