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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...
Autores principales: | Chakraborty, Debayan, Banerjee, Atreyee, Wales, David J. |
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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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