ArticleStructure (London, England : 1993)2017
Rotamer Libraries for the High-Resolution Design of β-Amino Acid Foldamers.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- FakeRotLib: Expedient Noncanonical Amino Acid Parametrization in Rosetta.Journal of chemical information and modeling · 2025Article
- Article
- Engineered coiled-coil HIF1α protein domain mimic.Biomaterials science · 2024Article
- Invariant point message passing for protein side chain packing.bioRxiv : the preprint server for biology · 2023Article
- An end-to-end deep learning method for protein side-chain packing and inverse folding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Exploiting Sequence-Dependent Rotamer Information in Global Optimization of Proteins.The journal of physical chemistry. B · 2022Article
- Engineering of enzymes using non-natural amino acids.Bioscience reports · 2022Review
- Study of Novel Peptides for Antimicrobial Protection in Solution and on Cotton Fabric.Molecules (Basel, Switzerland) · 2022Article
- Investigation of the structure-activity relationship in a series of new LVV- and VV-hemorphin-7 analogues designed as potential anticonvulsant agents.Amino acids · 2022Article
- Metal Cation-Binding Mechanisms of Q-Proline Peptoid Macrocycles in Solution.Journal of chemical information and modeling · 2021Article
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Authors and funding
5 authors.
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Abstract
β-Amino acids offer attractive opportunities to develop biologically active peptidomimetics, either employed alone or in conjunction with natural α-amino acids. Owing to their potential for unique conformational preferences that deviate considerably from α-peptide geometries, β-amino acids greatly expand the possible chemistries and physical properties available to polyamide foldamers. Complete in silico support for designing new molecules incorporating non-natural amino acids typically requires representing their side-chain conformations as sets of discrete rotamers for model refinement and sequence optimization. Such rotamer libraries are key components of several state-of-the-art design frameworks. Here we report the development, incorporation in to the Rosetta macromolecular modeling suite, and validation of rotamer libraries for β
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