In this section
@article{Youn:2022:10.1002/cbic.202200276,
author = {Youn, T and Yoon, S and Byrne, B and Chae, PS},
doi = {10.1002/cbic.202200276},
journal = {ChemBioChem: a European journal of chemical biology},
pages = {1--5},
title = {Foldable Detergents for Membrane Protein Stability},
url = {http://dx.doi.org/10.1002/cbic.202200276},
volume = {23},
year = {2022}
}
TY - JOUR
AB - Detergents are widely used for membrane protein structural study. Many recently developed detergents contain multiple tail and head groups, which are typically connected via a small and branched linker. Due to their inherent compact structures, with small inter-alkyl chain distances, these detergents form micelles with high alkyl chain density in the interiors, a feature favorably associated with membrane-protein stability. A recent study on tandem triazine maltosides (TZMs) revealed a distinct trend; despite possession of an apparently large inter-alkyl chain distance, the TZM−Es were highly effective at stabilizing membrane proteins. Thanks to the incorporation of a flexible spacer between the two triazine rings in the linker region, these detergents are prone to folding into a compact architecture in micellar environments instead of adopting an extended conformation. Detergent foldability represents a new concept of novel detergent design with significant potential for future detergent development.
AU - Youn,T
AU - Yoon,S
AU - Byrne,B
AU - Chae,PS
DO - 10.1002/cbic.202200276
EP - 5
PY - 2022///
SN - 1439-4227
SP - 1
TI - Foldable Detergents for Membrane Protein Stability
T2 - ChemBioChem: a European journal of chemical biology
UR - http://dx.doi.org/10.1002/cbic.202200276
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000820590100001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202200276
VL - 23
ER -
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