Abstract
The polarities of a large number of soluble and membrane proteins have been calculated by summing the mole fractions of polar amino acids. It was found that 85% of the 205 soluble proteins considered in this study had polarities of 47 ± 6%. Only 2% of the soluble proteins had polarities below 40%, whereas 47% of the 19 membrane proteins had polarities below 40%. The membrane proteins with polarities below 40% could be separated from their respective membranes only by detergents or organic solvents, indicating the importance of hydrophobic forces in their interaction with other membrane components. It is concluded that the majority of “intrinsic” membrane proteins have low polarity, and that the polarity index is therefore a useful parameter for characterization of membrane proteins.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 2:35 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 10:41 a.m.) |
Indexed | 3 weeks, 4 days ago (Aug. 5, 2025, 8:41 a.m.) |
Issued | 53 years, 4 months ago (April 1, 1972) |
Published | 53 years, 4 months ago (April 1, 1972) |
Published Online | 53 years, 4 months ago (April 1, 1972) |
Published Print | 53 years, 4 months ago (April 1, 1972) |
@article{Capaldi_1972, title={The Low Polarity of Many Membrane Proteins}, volume={69}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.69.4.930}, DOI={10.1073/pnas.69.4.930}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Capaldi, Roderick A. and Vanderkooi, Garret}, year={1972}, month=apr, pages={930–932} }