Crystallographic Characterization of N-Oxide Tripod Amphiphiles
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chae, Pil Seok | - |
dc.contributor.author | Guzei, Ilia A. | - |
dc.contributor.author | Gellman, Samuel H. | - |
dc.date.accessioned | 2021-06-23T13:38:33Z | - |
dc.date.available | 2021-06-23T13:38:33Z | - |
dc.date.created | 2021-01-21 | - |
dc.date.issued | 2010-02 | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/39974 | - |
dc.description.abstract | Tripod amphiphiles are designed to promote the solubilization and stabilization of intrinsic membrane proteins in aqueous solution; facilitation of crystallization is a long-range goal. Membrane proteins are subjects of extensive interest because of their critical biological roles, but proteins of this type can be difficult to study because of their low solubility in water. The nonionic detergents that are typically used to achieve solubility can have the unintended effect of causing protein denaturation. Tripod amphiphiles differ from conventional detergents in that the lipophilic segment contains a branchpoint, and previous work has shown that this unusual amphiphilic architecture can be advantageous relative to traditional detergent structures Here, we report the crystal structures of several tripod amphiphiles that contain an N-oxide hydrophilic group The data suggest that tripods can adapt themselves to a nonpolar surface by altering the hydrophobic appendage that projects toward that surface and their overall orientation relative to that surface Although it is not possible to draw firm conclusions regarding amphiphile association in solution from crystallographic data, trends observed among the packing patterns reported here suggest design strategies to be implemented in future studies | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | American Chemical Society | - |
dc.title | Crystallographic Characterization of N-Oxide Tripod Amphiphiles | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chae, Pil Seok | - |
dc.identifier.doi | 10.1021/ja9085148 | - |
dc.identifier.scopusid | 2-s2.0-77249144867 | - |
dc.identifier.wosid | 000275085000059 | - |
dc.identifier.bibliographicCitation | Journal of the American Chemical Society, v.132, no.6, pp.1953 - 1959 | - |
dc.relation.isPartOf | Journal of the American Chemical Society | - |
dc.citation.title | Journal of the American Chemical Society | - |
dc.citation.volume | 132 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 1953 | - |
dc.citation.endPage | 1959 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.subject.keywordPlus | MEMBRANE-PROTEIN CRYSTALLIZATION | - |
dc.subject.keywordPlus | PHOTOSYNTHETIC REACTION CENTER | - |
dc.subject.keywordPlus | HIGH-RESOLUTION STRUCTURE | - |
dc.subject.keywordPlus | CYTOCHROME-C-OXIDASE | - |
dc.subject.keywordPlus | ANGSTROM RESOLUTION | - |
dc.subject.keywordPlus | DETERGENT STRUCTURE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | CAPSID PROTEINS | - |
dc.subject.keywordPlus | OMPF PORIN | - |
dc.subject.keywordPlus | DESIGN | - |
dc.identifier.url | https://pubs.acs.org/doi/10.1021/ja9085148 | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
55 Hanyangdeahak-ro, Sangnok-gu, Ansan, Gyeonggi-do, 15588, Korea+82-31-400-4269 sweetbrain@hanyang.ac.kr
COPYRIGHT © 2021 HANYANG UNIVERSITY. ALL RIGHTS RESERVED.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.