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- W2084313676 abstract "We analyzed, based on the theoretical spectroscopic modeling, how the differences in the folding landscapes of two β-hairpin peptides trpzip2 and trpzip4 are reflected in their thermal unfolding infrared measurements. The isotope-edited equilibrium FTIR and two dimensional infrared spectra of the two peptides were calculated, using the nonlinear exciton propagation method, at a series of temperatures. The spectra calculations were based on the configuration distributions generated using the GBOBC implicit solvent MD simulation and the integrated tempering sampling technique. Conformational analysis revealed the different local thermal stabilities for these two peptides, which suggested the different folding landscapes. Our study further suggested that the ellipticities of the isotope peaks in the coherent IR signals are more sensitive to these local stability differences compared with other spectral features such as the peak intensities. Our technique can thus be combined with the relevant experimental measurements to achieve a better understanding of the peptide folding behaviors." @default.
- W2084313676 created "2016-06-24" @default.
- W2084313676 creator A5007016128 @default.
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- W2084313676 date "2014-02-05" @default.
- W2084313676 modified "2023-10-16" @default.
- W2084313676 title "Discriminating trpzip2 and trpzip4 peptides’ folding landscape using the two-dimensional infrared spectroscopy: A simulation study" @default.
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- W2084313676 doi "https://doi.org/10.1063/1.4863562" @default.
- W2084313676 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24511982" @default.
- W2084313676 hasPublicationYear "2014" @default.
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