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Role of Aromatic Cross-Links in Structure and Dynamics of Model Three-Stranded β-Sheet Peptides

Role of Aromatic Cross-Links in Structure and Dynamics of Model Three-Stranded β-Sheet Peptides

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SCHEERER, David, Heng CHI, Dan MCELHENY, Ayesha SAMER, Timothy A. KEIDERLING, Karin HAUSER, 2018. Role of Aromatic Cross-Links in Structure and Dynamics of Model Three-Stranded β-Sheet Peptides. In: The Journal of Physical Chemistry A. 122(2), pp. 543-553. ISSN 1089-5639. eISSN 1520-5215. Available under: doi: 10.1021/acs.jpca.7b10190

@article{Scheerer2018-01-18Aroma-41284, title={Role of Aromatic Cross-Links in Structure and Dynamics of Model Three-Stranded β-Sheet Peptides}, year={2018}, doi={10.1021/acs.jpca.7b10190}, number={2}, volume={122}, issn={1089-5639}, journal={The Journal of Physical Chemistry A}, pages={543--553}, author={Scheerer, David and Chi, Heng and McElheny, Dan and Samer, Ayesha and Keiderling, Timothy A. and Hauser, Karin} }

Samer, Ayesha Scheerer, David A series of closely related peptide sequences that form triple-strand structures was designed with a variation of cross-strand aromatic interactions and spectroscopically studied as models for β-sheet formation and stabilities. Structures of the three-strand models were determined with NMR methods and temperature-dependent equilibrium studies performed using circular dichroism and Fourier transform infrared spectroscopies. Our equilibrium data show that the presence of a direct cross-strand aromatic contact in an otherwise folded peptide does not automatically result in an increased thermal stability and can even distort the structure. The effect on the conformational dynamics was studied with infrared-detected temperature-jump relaxation methods and revealed a high sensitivity to the presence and the location of the aromatic cross-links. Aromatic contacts in the three-stranded peptides slow down the dynamics in a site-specific manner, and the impact seems to be related to the distance from the turn. With a Xxx-<sup>D</sup>Pro linkage as a probe with some sensitivity for the turn, small differences were revealed in the relative relaxation of the sheet strands and turn regions. In addition, we analyzed the component hairpins, which showed less uniform dynamics as compared to the parent three-stranded β-sheet peptides. Hauser, Karin McElheny, Dan Keiderling, Timothy A. McElheny, Dan 2018-02-09T12:58:56Z Samer, Ayesha Chi, Heng eng Hauser, Karin Role of Aromatic Cross-Links in Structure and Dynamics of Model Three-Stranded β-Sheet Peptides 2018-01-18 Keiderling, Timothy A. Chi, Heng 2018-02-09T12:58:56Z Scheerer, David

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