Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

A mass spectrometry-based approach to distinguish annular and specific lipid binding to membrane proteins

Tools
- Tools
+ Tools

Bolla, Jani Reddy, Corey, Robin A., Sahin, Cagla, Gault, Joseph, Hummer, Alissa, Hopper, Jonathan T. S., Lane, David P., Drew, David, Allison, Timothy M., Stansfeld, Phillip J., Robinson, Carol V. and Landreh, Michael (2020) A mass spectrometry-based approach to distinguish annular and specific lipid binding to membrane proteins. Angewandte Chemie International Edition, 59 (9). pp. 3523-3528. doi:10.1002/anie.201914411

[img]
Preview
PDF
WRAP-mass-spectrometry-based-approach-distinguish-annular-specific-lipid-binding-membrane-proteins-Stansfeld-2020.pdf - Published Version - Requires a PDF viewer.
Available under License Creative Commons Attribution 4.0.

Download (3051Kb) | Preview
[img] PDF
WRAP-mass-spectrometry-based-distinguish-Stansfeld-2020.pdf - Accepted Version
Embargoed item. Restricted access to Repository staff only - Requires a PDF viewer.

Download (6Mb)
Official URL: http://dx.doi.org/10.1002/anie.201914411

Request Changes to record.

Abstract

Membrane proteins engage in a variety of contacts with theirsurrounding lipids, but distinguishing between specifically boundlipids, and non-specific annular interactionsis a challenging problem. Applying native mass spectrometry to three membrane protein complexes with different lipid binding properties, we explore the ability of detergents to compete with lipids bound in different environments. We show that lipids in annular positions on the Presenilin Homologue protease are subject to constant exchange with detergent. Bycontrast,detergent-resistantlipids bound at the dimer interface in the Leucine transportershowdecreased koffrates in molecular dynamics simulations.Turning tothe lipid flippase MurJ, we findthat addition of the natural substrate lipid-II results in the formation of a 1:1 protein-lipid complex, where the lipid cannot be displaced by detergentfromthe highly protected active site.In summary, we distinguish annular from non-annular lipids based on their exchange rates in solution. [Abstract copyright: © 2019 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.]

Item Type: Journal Article
Subjects: Q Science > QC Physics
Q Science > QD Chemistry
Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
SWORD Depositor: Library Publications Router
Library of Congress Subject Headings (LCSH): Mass spectrometry, Lipids, Molecular dynamics, Membrane proteins
Journal or Publication Title: Angewandte Chemie International Edition
Publisher: Wiley
ISSN: 1433-7851
Official Date: 24 February 2020
Dates:
DateEvent
24 February 2020Published
30 December 2019Available
30 December 2019Accepted
Volume: 59
Number: 9
Page Range: pp. 3523-3528
DOI: 10.1002/anie.201914411
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
UNSPECIFIEDSwedish Foundation for International Cooperation in Research and Higher Educationhttp://dx.doi.org/10.13039/501100001728
UNSPECIFIEDKarolinska Institutethttp://dx.doi.org/10.13039/501100004047
2013_08807Vetenskapsrådethttp://dx.doi.org/10.13039/501100004359
104633/Z/14/Wellcome Trusthttp://dx.doi.org/10.13039/100010269
641317[ERC] Horizon 2020 Framework Programmehttp://dx.doi.org/10.13039/100010661
MR/N020413/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
208361/Z/17/Wellcome Trusthttp://dx.doi.org/10.13039/100010269
BB/P01948X/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/R002517/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/S003339/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
EP/R029407/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us