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Accessible Surfaces of Beta Proteins Increase with Increasing Protein Molecular Mass More Rapidly than Those of Other Proteinsстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 4 марта 2022 г.
- Авторы: Glyakina Anna V., Bogatyreva Natalya S., Galzitskaya Oxana V.
- Журнал: PLoS ONE
- Том: 6
- Номер: 12
- Год издания: 2011
- Издательство: Public Library of Science
- Местоположение издательства: United States
- Первая страница: e28464
- DOI: 10.1371/journal.pone.0028464
- Аннотация: Here we present a systematic analysis of accessible surface areas and hydrogen bonds of 2554 globular proteins from four structural classes (all-alpha, all-beta, alpha/beta and alpha+beta proteins) that is aimed to learn in which structural class the accessible surface area increases with increasing protein molecular mass more rapidly than in other classes, and what structural peculiarities are responsible for this effect. The beta structural class of proteins was found to be the leader, with the following possible explanations of this fact. First, in beta structural proteins, the fraction of residues not included in the regular secondary structure is the largest, and second, the accessible surface area of packaged elements of the beta-structure increases more rapidly with increasing molecular mass in comparison with the alpha-structure. Moreover, in the beta structure, the probability of formation of backbone hydrogen bonds is higher than that in the alpha helix for all residues of alpha+beta proteins (the average probability is 0.73 +/- 0.01 for the beta-structure and 0.60 +/- 0.01 for the alpha-structure without proline) and alpha/beta proteins, except for asparagine, aspartic acid, glycine, threonine, and serine (0.70 +/- 0.01 for the beta-structure and 0.60 +/- 0.01 for the alpha-structure without the proline residue). There is a linear relationship between the number of hydrogen bonds and the number of amino acid residues in the protein (Number of hydrogen bonds=0.678: number of residues=3.350).
- Добавил в систему: Галзитская Оксана Валериановна