Trifluoroethanol stabilizes the molten globule state and induces non-amyloidic turbidity in stem bromelain near its isoelectric point

Dave, Sandeep; Mahajan, Sahil; Chandra, Vemika; Gupta, Pawan

doi:10.1016/j.ijbiomac.2011.06.006

Cited by 9 publications

(1 citation statement)

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“…For example, the 2,2,2-trifluoroethanol (TFE) has been shown to stabilize/induce the formation of helical conformations in denatured proteins. 6,7 In the field of protein folding, molecular dynamics (MD) simulation is considered as a powerful tool for elucidating the folding dynamics, [8][9][10][11][12] such as acquiring early folding events and ensembles during the self-assembly of proteins to their biological "native state" unbiased by native-state information. However, most folding studies, thus far, sample the complete phase space in order to find the native structure.…”

Section: Introductionmentioning

confidence: 99%

Solvent effect on the folding dynamics and structure of E6-associated protein characterized from ab initio protein folding simulations

Lazim

Sun

et al. 2012

The Journal of Chemical Physics

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Solvent effect on protein conformation and folding mechanism of E6-associated protein (E6ap) peptide are investigated using a recently developed charge update scheme termed as adaptive hydrogen bond-specific charge (AHBC). On the basis of the close agreement between the calculated helix contents from AHBC simulations and experimental results, we observed based on the presented simulations that the two ends of the peptide may simultaneously take part in the formation of the helical structure at the early stage of folding and finally merge to form a helix with lowest backbone RMSD of about 0.9 Å in 40% 2,2,2-trifluoroethanol solution. However, in pure water, the folding may start at the center of the peptide sequence instead of at the two opposite ends. The analysis of the free energy landscape indicates that the solvent may determine the folding clusters of E6ap, which subsequently leads to the different final folded structure. The current study demonstrates new insight to the role of solvent in the determination of protein structure and folding dynamics.

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