ArticleProteins2019
Sequence-specific dynamic information in proteins.
Article in Proteins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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
6 citing papers in PubMed.
- The Spatial Distribution of Local Mobility in Folded Proteins.The journal of physical chemistry. B · 2026Article
- Techniques for Bioinformatic Applications in Protein Dynamics.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Application of artificial intelligence and machine learning techniques to the analysis of dynamic protein sequences.Proteins · 2024Article
- The dynamic basis of structural order in proteins.Proteins · 2022Article
- Dynamic and conformational switching in proteins.Biopolymers · 2021Article
- The structure of protein dynamic space.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
2 authors.
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Abstract
We examine the local and global properties of the average B-factor, 〈B〉, as a residue-specific indicator of protein dynamic characteristics. It has been shown that values of 〈B〉 for the 20 amino acids differ in a statistically significant manner, and that, while strongly determined by the static physical properties of amino acids, they also encode averaged information about the influence of global fold on single-residue dynamics. Therefore, complete sequences of amino acids also encode fold-related global dynamic information, in addition to the local information that arises from static physical properties. We show that the relative magnitudes of these two contributions can be determined using Fourier methods, which represent the global properties of the sequences. It has also been shown that the behavior of Fourier components of 〈B〉 differs, with very high statistical significance, between structural groups, and that this information is not available from a comparable analysis of static amino acid properties.
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Registered trials
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