How well does cholesteryl hemisuccinate mimic cholesterol in saturated phospholipid bilayers?
| Autor: | Joona Tynkkynen, Waldemar Kulig, Moutusi Manna, Ilpo Vattulainen, Matti Javanainen, Pavel Jungwirth, Tomasz Róg |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Cholesteryl hemisuccinate
Lipid Bilayers Phospholipid Molecular Dynamics Simulation Catalysis law.invention Inorganic Chemistry Molecular dynamics chemistry.chemical_compound law polycyclic compounds Membrane protein crystallization Organic chemistry Physical and Theoretical Chemistry Crystallization Phospholipids Cholesterol Cell Membrane Organic Chemistry Lipids Computer Science Applications Membrane Computational Theory and Mathematics Membrane protein chemistry Biophysics lipids (amino acids peptides and proteins) Cholesterol Esters |
| Zdroj: | Journal of Molecular Modeling Kulig, W, Tynkkynen, J, Javanainen, M, Manna, M, Rog, T, Vattulainen, I & Jungwirth, P 2014, ' How well does cholesteryl hemisuccinate mimic cholesterol in saturated phospholipid bilayers? ', Journal of Molecular Modeling, vol. 20, no. 2, 2121 . https://doi.org/10.1007/s00894-014-2121-z |
| ISSN: | 1610-2940 |
| DOI: | 10.1007/s00894-014-2121-z |
| Popis: | Cholesteryl hemisuccinate is a detergent that is often used to replace cholesterol in crystallization of membrane proteins. Here we employ atomistic molecular dynamics simulations to characterize how well the properties of cholesteryl hemisuccinate actually match those of cholesterol in saturated protein-free lipid membranes. We show that the protonated form of cholesteryl hemisuccinate mimics many of the membrane properties of cholesterol quite well, while the deprotonated form of cholesteryl hemisuccinate is less convincing in this respect. Based on the results, we suggest that cholesteryl hemisuccinate in its protonated form is a quite faithful mimic of cholesterol for membrane protein crystallization, if specific cholesterol-protein interactions (not investigated here) are not playing a crucial role. |
| Databáze: | OpenAIRE |
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