Side-Chain Polarity Modulates the Intrinsic Conformational Landscape of Model Dipeptides
نویسندگان
چکیده
The intrinsic conformational preferences of small peptides may provide additional insight into the thermodynamics and kinetics protein folding. In this study, we explore underlying energy landscapes two model peptides, namely, Ac-Ala-NH2 Ac-Ser-NH2, using geometry-optimization-based tools developed within context landscape theory. We analyze not only how side-chain polarity influences structural dipeptides, but also other emergent properties landscape, including heat capacity profiles, rearrangements. contrasting topographies free agree with recent results from Fourier transform microwave spectroscopy experiments, where was found to exist as a mixture conformers, while Ac-Ser-NH2 remained structurally locked, despite exhibiting an apparently rich landscape.
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ژورنال
عنوان ژورنال: Journal of Physical Chemistry B
سال: 2021
ISSN: ['1520-6106', '1520-5207']
DOI: https://doi.org/10.1021/acs.jpcb.1c02412