ReviewMethods in molecular biology (Clifton, N.J.)2018
Solid-State NMR Structural Characterization of Self-Assembled Peptides with Selective
Review in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Advances in Antimicrobial Peptides: Mechanisms, Design Innovations, and Biomedical Potential.Molecules (Basel, Switzerland) · 2025Review
- Parallel β-Sheet Structure and Structural Heterogeneity Detected within Q11 Self-Assembling Peptide Nanofibers.The journal of physical chemistry. B · 2024Article
- Structural Consequences of Introducing Bioactive Domains to Designer β-Sheet Peptide Self-Assemblies.Biomacromolecules · 2024Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
For the structural characterization methods discussed here, information on molecular conformation and intermolecular organization within nanostructured peptide assemblies is discerned through analysis of solid-state NMR spectral features. This chapter reviews general NMR methodologies, requirements for sample preparation, and specific descriptions of key experiments. An attempt is made to explain choices of solid-state NMR experiments and interpretation of results in a way that is approachable to a nonspecialist. Measurements are designed to determine precise NMR peak positions and line widths, which are correlated with secondary structures, and probe nuclear spin-spin interactions that report on three-dimensional organization of atoms. The formulation of molecular structural models requires rationalization of data sets obtained from multiple NMR experiments on samples with carefully chosen
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Registered trials
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