Transmembrane channel activity of gramicidin A analogs: Effects of modification and deletion of the amino-terminal residue
β Scribed by J.S. Morrow; W.R. Veatch; L. Stryer
- Book ID
- 118918120
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 404 KB
- Volume
- 132
- Category
- Article
- ISSN
- 0022-2836
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π SIMILAR VOLUMES
Using the previously reported ab initio interaction energies among K ' , Na+, water, and Gramicidin A (GA), this report presents Monte Carlo simulations for the microscopic effect of an applied voltage (0.5 V/32 A) on a solvated gramicidin. The reorientation of water molecules due to the applied vol
## Abstract Transmembrane domains (TMDs) of Gβprotein coupled receptors (GPCRs) have very low water solubility and often aggregate during purification and biophysical investigations. To circumvent this problem many laboratories add oligolysines to the __N__β and __C__βtermini of peptides that corre