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Side-Chain Polarity Modulates the Intrinsic Conformational Landscape of Model Dipeptides

[Image: see text] The intrinsic conformational preferences of small peptides may provide additional insight into the thermodynamics and kinetics of protein folding. In this study, we explore the underlying energy landscapes of two model peptides, namely, Ac-Ala-NH(2) and Ac-Ser-NH(2), using geometry...

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Detalles Bibliográficos
Autores principales: Chakraborty, Debayan, Banerjee, Atreyee, Wales, David J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8279551/
https://www.ncbi.nlm.nih.gov/pubmed/34037392
http://dx.doi.org/10.1021/acs.jpcb.1c02412

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