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Cyclohexyl-α maltos...
Cyclohexyl-α maltoside as a highly efficient tool for membrane protein studies
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- Missel, Julie Winkel (författare)
- University of Copenhagen
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- Salustros, Nina (författare)
- University of Copenhagen
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- Becares, Eva Ramos (författare)
- University of Copenhagen
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- Steffen, Jonas Hyld (författare)
- University of Copenhagen
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- Laursen, Amalie Gerdt (författare)
- University of Copenhagen
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- Garcia, Angelica Struve (författare)
- European Molecular Biology Laboratory Hamburg
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- Garcia-Alai, Maria M. (författare)
- Centre for Structural Systems Biology (CSSB),European Molecular Biology Laboratory Hamburg
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- Kolar, Čeněk (författare)
- Glycon Biochemicals GmbH
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- Gourdon, Pontus (författare)
- Lund University,Lunds universitet,Membranproteinstrukturbiologi,Forskargrupper vid Lunds universitet,Membrane Protein Structural Biology,Lund University Research Groups,University of Copenhagen
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- Gotfryd, Kamil (författare)
- University of Copenhagen
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(creator_code:org_t)
- Elsevier BV, 2021
- 2021
- Engelska 10 s.
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Ingår i: Current Research in Structural Biology. - : Elsevier BV. - 2665-928X. ; 3, s. 85-94
- Relaterad länk:
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http://dx.doi.org/10... (free)
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https://doi.org/10.1...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Membrane proteins (MPs) constitute a large fraction of the proteome, but exhibit physicochemical characteristics that impose challenges for successful sample production crucial for subsequent biophysical studies. In particular, MPs have to be extracted from the membranes in a stable form. Reconstitution into detergent micelles represents the most common procedure in recovering MPs for subsequent analysis. n-dodecyl-β-D-maltoside (DDM) remains one of the most popular conventional detergents used in production of MPs. Here we characterize the novel DDM analogue 4-trans-(4-trans-propylcyclohexyl)-cyclohexyl α-maltoside (t-PCCαM), possessing a substantially lower critical micelle concentration (CMC) than the parental compound that represents an attractive feature when handling MPs. Using three different types of MPs of human and prokaryotic origin, i.e., a channel, a primary and a secondary active transporter, expressed in yeast and bacterial host systems, respectively, we investigate the performance of t-PCCαM in solubilization and affinity purification together with its capacity to preserve native fold and activity. Strikingly, t-PCCαM displays favorable behavior in extracting and stabilizing the three selected targets. Importantly, t-PCCαM promoted extraction of properly folded protein, enhanced thermostability and provided negatively-stained electron microscopy samples of promising quality. All-in-all, t-PCCαM emerges as competitive surfactant applicable to a broad portfolio of challenging MPs for downstream structure-function analysis.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Cryo-EM
- Crystallization
- Detergent
- Membrane proteins
- Solubilization
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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Missel, Julie Wi ...
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Salustros, Nina
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Becares, Eva Ram ...
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Steffen, Jonas H ...
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Laursen, Amalie ...
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Garcia, Angelica ...
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visa fler...
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Garcia-Alai, Mar ...
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Kolar, Čeněk
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Gourdon, Pontus
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Gotfryd, Kamil
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- NATURVETENSKAP
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Lunds universitet