NDLI: Dodecylphosphocholine micelles as a membrane-like environment: new results from NMR relaxation and paramagnetic relaxation enhancement analysis

Please wait, while we are loading the content...

Resonance Raman investigation of lysine and N-acetylmethionine complexes of ferric and ferrous microperoxidase : Influences of the axial ligation on the heme c structure

Cell adhesion monitoring using a quartz crystal microbalance: comparative analysis of different mammalian cell lines

Hydrodynamic properties of mucins secreted by primary cultures of Guinea-pig tracheal epithelial cells: determination of diffusion coefficients by analytical ultracentrifugation and kinetic analysis of mucus gel hydration and dissolution

Dodecylphosphocholine micelles as a membrane-like environment: new results from NMR relaxation and paramagnetic relaxation enhancement analysis

Effects of pulmonary surfactant proteins SP-B and SP-C and calcium ions on the surface properties of hydrophobic fractions of lung surfactant

Numerical simulation of aldolase tetramer stability

A mechanism for the establishment of polar cell morphology based on the cytoskeleton-derived forces exerted on the cell boundary

Wide applicability of a flow cytometric assay to measure absolute membrane potentials on the millivolt scale

Structural descriptions of ligands in their binding site of integral membrane proteins at near physiological conditions using solid-state NMR

European Biophysics Journal : Volume 27

European Biophysics Journal : Volume 26

European Biophysics Journal : Volume 25

Dodecylphosphocholine micelles as a membrane-like environment: new results from NMR relaxation and paramagnetic relaxation enhancement analysis

Content Provider	Springer Nature Link
Author	Beswick, Veronica Guerois, Raphaël Cordier Ochsenbein, Françoise Coïc, Yves Marie Huynh Dinh, Tam Tostain, Jean ël, Jean Pierre Sanson, Alain Neumann, J. M.
Copyright Year	1998
Abstract	To further examine to what extent a dodecylphosphocholine (DPC) micelle mimics a phosphatidylcholine bilayer environment, we performed 13C, 2H, and 31P NMR relaxation measurements. Our data show that the dynamic behavior of DPC phosphocholine groups at low temperature (12 °C) corresponds to that of a phosphatidylcholine interface at high temperature (51 °C). In the presence of helical peptides, a PMP1 fragment, or an annexin fragment, the DPC local dynamics are not affected whereas the DPC aggregation number is increased to match an appropriate area/volume ratio for accommodating the bound peptides. We also show that quantitative measurements of paramagnetic relaxation enhancements induced by small amounts of spin-labeled phospholipids on peptide proton signals provide a meaningful insight on the location of both PMP1 and annexin fragments in DPC micelles. The paramagnetic contributions to the relaxation were extracted from intra-residue cross-peaks of NOESY spectra for both peptides. The location of each peptide in the micelles was found consistent with the corresponding relaxation data. As illustrated by the study of the PMP1 fragment, paramagnetic relaxation data also allow us to supply the missing medium-range NOEs and therefore to complete a standard conformational analysis of peptides in micelles.
Starting Page	48
Ending Page	58
Page Count	11
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	28
Issue Number	1
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-11-27
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

A decadentate Gd(III)-coordinating paramagnetic cosolvent for protein relaxation enhancement measurement

Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide

Efficient DNP NMR of membrane proteins: sample preparation protocols, sensitivity, and radical location

Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes

Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome–nascent chain complexes

Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement

Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis

Structure determination of uniformly $^{13}$C, $^{15}$N labeled protein using qualitative distance restraints from MAS solid-state $^{13}$C-NMR observed paramagnetic relaxation enhancement

Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen

Dodecylphosphocholine micelles as a membrane-like environment: new results from NMR relaxation and paramagnetic relaxation enhancement analysis

Similar Documents

A decadentate Gd(III)-coordinating paramagnetic cosolvent for protein relaxation enhancement measurement

Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide

Efficient DNP NMR of membrane proteins: sample preparation protocols, sensitivity, and radical location

Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes

Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome–nascent chain complexes

Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement

Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis

Structure determination of uniformly $^{13}$C, $^{15}$N labeled protein using qualitative distance restraints from MAS solid-state $^{13}$C-NMR observed paramagnetic relaxation enhancement

Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen

Dodecylphosphocholine micelles as a membrane-like environment: new results from NMR relaxation and paramagnetic relaxation enhancement analysis