Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00458857" target="_blank" >RIV/61388963:_____/16:00458857 - isvavai.cz</a>
Result on the web
<a href="http://www.nature.com/articles/srep21759" target="_blank" >http://www.nature.com/articles/srep21759</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/srep21759" target="_blank" >10.1038/srep21759</a>
Alternative languages
Result language
angličtina
Original language name
Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels
Original language description
Gating charges in voltage-sensing domains (VSD) of voltage-sensitive ion channels and enzymes are carried on arginine side chains rather than lysine. This arginine preference may result from the unique hydration properties of the side chain guanidinium group which facilitates its movement through a hydrophobic plug that seals the center of the VSD, as suggested by molecular dynamics simulations. To test for side chain interactions implicit in this model we inspected interactions of the side chains of arginine and lysine with each of the 19 non-glycine amino acids in proteins in the protein data bank. The arginine guanidinium interacts with non-polar aromatic and aliphatic side chains above and below the guanidinium plane while hydrogen bonding with polar side chains is restricted to in-plane positions. In contrast, non-polar side chains interact largely with the aliphatic part of the lysine side chain. The hydration properties of arginine and lysine are strongly reflected in their respective interactions with non-polar and polar side chains as observed in protein structures and in molecular dynamics simulations, and likely underlie the preference for arginine as a mobile charge carrier in VSD.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
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Volume of the periodical
6
Issue of the periodical within the volume
Feb 22
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
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UT code for WoS article
000370513000001
EID of the result in the Scopus database
2-s2.0-84959160794