期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 5, 页码 1692-1695出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1215400110
关键词
GWALP23; lysine titration; solid-state deuterium NMR
资金
- US National Science Foundation [MCB 0841227]
- Arkansas Biosciences Institute
- National Institutes of Health [GM103429, GM103450]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0841227] Funding Source: National Science Foundation
The ionization states of individual amino acid residues of membrane proteins are difficult to decipher or assign directly in the lipid bilayer membrane environment We address this issue for lysines and arginines in designed transmembrane helices. For lysines (but not arginines) at two locations within dioleoyl-phosphatidylcholine bilayer membranes, we measure pK(a) values below 7.0. We find that buried charged lysine, in fashion similar to arginine, will modulate helix orientation to maximize its own access to the aqueous interface or, if occluded by aromatic rings, may cause a transmembrane helix to exit the lipid bilayer. Interestingly, the influence of neutral lysine (vis-a-vis leucine) upon helix orientation also,depends upon its aqueous access. Our results suggest that changes in the ionization states of particular residues will regulate membrane protein function and furthermore illustrate the subtle complexity of ionization behavior with respect to the detailed lipid and protein environment.
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