English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.

Weingarth, M., Ader, C., Melquiond, A. J. S., Nand, D., Pong, O., Becker, S., et al. (2012). Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations. Biophysical Journal, 103(1), 29-37. doi:10.1016/j.bpj.2012.05.016.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-EEF1-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-357E-F
Genre: Journal Article

Files

show Files
hide Files
:
1542193.pdf (Publisher version), 1004KB
Name:
1542193.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1542193-Suppl-1.pdf (Supplementary material), 2MB
Name:
1542193-Suppl-1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1542193-Suppl-2.zip (Supplementary material), 2MB
Name:
1542193-Suppl-2.zip
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/zip / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Weingarth, M., Author
Ader, C., Author
Melquiond, A. J. S., Author
Nand, D., Author
Pong, O., Author
Becker, S.1, Author              
Bonvin, A. M. J. J., Author
Baldus, M., Author
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

Content

show
hide
Free keywords: -
 Abstract: Elemental biological functions such as molecular signal transduction are determined by the dynamic interplay between polypeptides and the membrane environment. Determining such supramolecular arrangements poses a significant challenge for classical structural biology methods. We introduce an iterative approach that combines magic-angle spinning solid-state NMR spectroscopy and atomistic molecular dynamics simulations for the determination of the structure and topology of membrane-bound systems with a resolution and level of accuracy difficult to obtain by either method alone. Our study focuses on the Shaker B ball peptide that is representative for rapid N-type inactivating domains of voltage-gated K+ channels, associated with negatively charged lipid bilayers.

Details

show
hide
Language(s): eng - English
 Dates: 2012-07-03
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2012.05.016
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biophysical Journal
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 103 (1) Sequence Number: - Start / End Page: 29 - 37 Identifier: -