| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7692441 | Chemistry and Physics of Lipids | 2013 | 12 Pages |
Abstract
⺠Membrane deformation cannot alleviate completely the hydrophobic mismatch in multi-TM proteins. ⺠A non-conserved membrane-facing residue K288 in LeuT causes large membrane deformation. ⺠Water penetration and membrane bending near K288 affects neighboring hydrophobic residues. ⺠The cost of mismatch at TM1a impedes its outward movement required for function. ⺠Effect of residual hydrophobic mismatch at TM1a is eliminated in the K288A mutant and transport efficiency is increased.
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Authors
Sayan Mondal, George Khelashvili, Lei Shi, Harel Weinstein,