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Transmembrane helices containing a charged arginine are thermodynamically stable
Hydrophobic amino acids are abundant in transmembrane (TM) helices of membrane proteins. Charged residues are sparse, apparently due to the unfavorable energetic cost of partitioning charges into non-polar phases. Nevertheless, conserved arginine residues within TM helices regulate vital functions,...
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| Опубликовано в: : | Eur Biophys J |
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| Главные авторы: | , , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2017
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5640460/ https://ncbi.nlm.nih.gov/pubmed/28409218 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s00249-017-1206-x |
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