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.

• MeSH
• arginin chemie   MeSH
• databáze proteinů MeSH
• draslíkový kanál ERG1 chemie   MeSH
• gating iontového kanálu MeSH
• guanidin chemie   MeSH
• hydrofobní a hydrofilní interakce MeSH
• lidé MeSH
• lysin chemie   MeSH
• protein - isoformy chemie   MeSH
• sekvence aminokyselin MeSH
• simulace molekulární dynamiky * MeSH
• statická elektřina MeSH
• strukturní homologie proteinů MeSH
• voda chemie   MeSH
• vodíková vazba MeSH
• vztahy mezi strukturou a aktivitou MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH