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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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Bibliografske podrobnosti
izdano v:Eur Biophys J
Main Authors: Ulmschneider, Martin B., Ulmschneider, Jakob P., Freites, J. Alfredo, von Heijne, Gunnar, Tobias, Douglas J., White, Stephen H.
Format: Artigo
Jezik:Inglês
Izdano: 2017
Teme:
Online dostop: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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