Sequence-specific dynamic information in proteins
| Autor: | S. Rackovsky, Harold A. Scheraga |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Protein Folding
Fold (higher-order function) Protein Conformation ENCODE Biochemistry Article 03 medical and health sciences symbols.namesake Protein Domains Structural Biology Sequence Analysis Protein Humans Amino Acids Molecular Biology 030304 developmental biology Sequence (medicine) chemistry.chemical_classification 0303 health sciences Protein dynamics 030302 biochemistry & molecular biology Computational Biology Proteins Amino acid Fourier transform chemistry symbols Biological system Algorithms |
| Zdroj: | Proteins |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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