ArticleJournal of the American Chemical Society2024
Rapid Quantification of Protein Secondary Structure Composition from a Single Unassigned 1D
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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Who cites it
4 citing papers in PubMed.
- Real-time electrical monitoring of enzymatic catalytic dynamics at the single-molecule level.Nature communications · 2026Article
- Article
- Multivariate Chemometric and FTIR Insights Into the Effects of Rice Bran Extracts on Brown Rice Protein Bars.Food science & nutrition · 2026Article
- Prediction of Protein Secondary Structures Based on Substructural Descriptors of Molecular Fragments.International journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The function of a protein is predicated upon its three-dimensional fold. Representing its complex structure as a series of repeating secondary structural elements is one of the most useful ways by which we study, characterize, and visualize a protein. Consequently, experimental methods that quantify the secondary structure content allow us to connect a protein's structure to its function. Here, we introduce an automated gradient descent-based method we refer to as secondary-structure distribution by NMR that allows for rapid quantification of the protein secondary structure composition of a protein from a single, 1D
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