The University of Southampton
University of Southampton Institutional Repository

Towards dipolar recoupling in macroscopically ordered samples of membrane proteins rotating at the magic angle

Towards dipolar recoupling in macroscopically ordered samples of membrane proteins rotating at the magic angle
Towards dipolar recoupling in macroscopically ordered samples of membrane proteins rotating at the magic angle
MAS NMR spectroscopy can be combined with the advantages of uniaxially ordered samples of membrane proteins as demonstrated in the so-called MAOSS (magic angle oriented sample spinning) experiment. Under these conditions, dipolar recoupling methods can be used to determine the orientation of internuclear vectors with respect to the MAS rotor frame.
However, most approaches to measure dipolar couplings yield angle ambiguities even in the static, non-spinning case. Here, we present the possibility to overcome these problems by deriving a new homonuclear double-quantum radio frequency pulse sequence based on an eightfold symmetry. Only dipolar Hamiltonian terms with spatial components m=±2 are recoupled with high efficiency allowing unambiguous angle determinations. Preliminary data demonstrate the applicability to oriented samples.
079237102X
71-83
Kluwer Academic Publishers
Glaubitz, Clemens
99f5e847-e6fd-4783-bc60-054bf0e15661
Carravetta, Marina
1b12fa96-4a6a-4689-ab3b-ccc68f1d7691
Edén, Mattias
b51e4e79-5ef3-4d12-abcf-d08a290c1c8c
Levitt, Malcolm H.
bcc5a80a-e5c5-4e0e-9a9a-249d036747c3
Kiihne, S.R.
de Groot, H.J.M.
Glaubitz, Clemens
99f5e847-e6fd-4783-bc60-054bf0e15661
Carravetta, Marina
1b12fa96-4a6a-4689-ab3b-ccc68f1d7691
Edén, Mattias
b51e4e79-5ef3-4d12-abcf-d08a290c1c8c
Levitt, Malcolm H.
bcc5a80a-e5c5-4e0e-9a9a-249d036747c3
Kiihne, S.R.
de Groot, H.J.M.

Glaubitz, Clemens, Carravetta, Marina, Edén, Mattias and Levitt, Malcolm H. (2001) Towards dipolar recoupling in macroscopically ordered samples of membrane proteins rotating at the magic angle. In, Kiihne, S.R. and de Groot, H.J.M. (eds.) Perspectives on Solid State NMR in Biology. (Focus on Structural Biology, 1) Dordrecht, The Netherlands. Kluwer Academic Publishers, pp. 71-83.

Record type: Book Section

Abstract

MAS NMR spectroscopy can be combined with the advantages of uniaxially ordered samples of membrane proteins as demonstrated in the so-called MAOSS (magic angle oriented sample spinning) experiment. Under these conditions, dipolar recoupling methods can be used to determine the orientation of internuclear vectors with respect to the MAS rotor frame.
However, most approaches to measure dipolar couplings yield angle ambiguities even in the static, non-spinning case. Here, we present the possibility to overcome these problems by deriving a new homonuclear double-quantum radio frequency pulse sequence based on an eightfold symmetry. Only dipolar Hamiltonian terms with spatial components m=±2 are recoupled with high efficiency allowing unambiguous angle determinations. Preliminary data demonstrate the applicability to oriented samples.

Text
LeidenGlaubitz.pdf - Other
Download (502kB)

More information

Published date: 2001

Identifiers

Local EPrints ID: 27760
URI: http://eprints.soton.ac.uk/id/eprint/27760
ISBN: 079237102X
PURE UUID: 469c9177-1190-4f47-ab9e-a0ab583e9c27
ORCID for Marina Carravetta: ORCID iD orcid.org/0000-0002-6296-2104
ORCID for Malcolm H. Levitt: ORCID iD orcid.org/0000-0001-9878-1180

Catalogue record

Date deposited: 26 Apr 2006
Last modified: 20 Mar 2024 02:38

Export record

Contributors

Author: Clemens Glaubitz
Author: Mattias Edén
Editor: S.R. Kiihne
Editor: H.J.M. de Groot

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×