TY - JOUR AU - 김진웅 DA - 2014/11 PY - 2014 UR - http://pubs.rsc.org/en/Content/ArticleLanding/2014/OB/C4OB01375A#!divAbstract UR - http://hdl.handle.net/20.500.11754/51266 AB - Detergents are widely used for membrane protein research; however, membrane proteins encapsulated in micelles formed by conventional detergents tend to undergo structural degradation, necessitating the development of new agents with enhanced efficacy. Here we prepared several hydrophobic variants of ganglio-tripod amphiphiles (TPAs) derived from previously reported TPAs and evaluated for a multi-subunit, pigment protein superassembly. In this study. TPA-16 was found to be most efficient in protein solubilization while TPA-15 proved most favourable in long-term protein stability. The current study combined with previous TPA studies enabled us to elaborate on a few detergent structure-property relationships that could provide useful guidelines for novel amphiphile design. PB - ROYAL SOC CHEMISTRY, THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND KW - MUSCARINIC ACETYLCHOLINE-RECEPTOR TI - New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure-property relationships VL - 12 DO - 10.1039/c4ob01375a T2 - ORGANIC & BIOMOLECULAR CHEMISTRY ER -