Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm: Application to phospholamban

Alessandro Mascioni; Becky L. Eggimann; Gianluigi Veglia

doi:10.1016/j.chemphyslip.2004.09.018

Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm: Application to phospholamban

Alessandro Mascioni, Becky L. Eggimann, Gianluigi Veglia

Chemical and Structural Biology (TMED)

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

Dipolar waves are distinct hallmarks of both the secondary and tertiary structures of α-helical proteins that are immobilized in membrane bilayers or embedded in anisotropic media. We present a simple, semi-empirical approach that exploits the modulation of the amplitude and average of dipolar waves to determine the topology of α-helical proteins. Moreover, we describe the application of this method for the structural determination of a detergent solubilized membrane protein, phospholamban (PLB) that is involved in calcium regulation of cardiac muscle. When combined with high-resolution solid-state NMR data, this method can serve as a fast route for determining the topology of helical membrane proteins solubilized in detergent micelles.

Original language	English (US)
Pages (from-to)	133-144
Number of pages	12
Journal	Chemistry and Physics of Lipids
Volume	132
Issue number	1
DOIs	https://doi.org/10.1016/j.chemphyslip.2004.09.018
State	Published - Oct 2004

Bibliographical note

Funding Information:
This work was supported in part by grants to G.V. (NIH GM64742; AHA 0160465Z). The authors would like to thank Dr. S.J. Opella, Francesca Marassi, Michael Mesleh for many helpful discussions, Roberto Di Fonzo for encouragement and support, David Live and Beverly Ostrowski for help with NMR experiments. We also benefited from the facilities at the Minnesota High-Field NMR Center in the Department of Biochemistry, Molecular Biology, and Biophysics; University of Minnesota. NMR instrumentation was provided with funds from the NSF (BIR-961477) and the University of Minnesota Medical School.

Keywords

Ca-ATPase
DPC micelles
Dipolar waves
Exhaustive search
Helical wheels
Membrane proteins
NMR
Phospholamban
Polyacrylamide gel
Residual dipolar couplings
SERCA
α-Helix

Access

10.1016/j.chemphyslip.2004.09.018

OpenUrl availability

Full text

Cite this

@article{7ee15e772a0e4fada7ef28f135a594ca,

title = "Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm: Application to phospholamban",

abstract = "Dipolar waves are distinct hallmarks of both the secondary and tertiary structures of α-helical proteins that are immobilized in membrane bilayers or embedded in anisotropic media. We present a simple, semi-empirical approach that exploits the modulation of the amplitude and average of dipolar waves to determine the topology of α-helical proteins. Moreover, we describe the application of this method for the structural determination of a detergent solubilized membrane protein, phospholamban (PLB) that is involved in calcium regulation of cardiac muscle. When combined with high-resolution solid-state NMR data, this method can serve as a fast route for determining the topology of helical membrane proteins solubilized in detergent micelles.",

keywords = "Ca-ATPase, DPC micelles, Dipolar waves, Exhaustive search, Helical wheels, Membrane proteins, NMR, Phospholamban, Polyacrylamide gel, Residual dipolar couplings, SERCA, α-Helix",

author = "Alessandro Mascioni and Eggimann, {Becky L.} and Gianluigi Veglia",

note = "Funding Information: This work was supported in part by grants to G.V. (NIH GM64742; AHA 0160465Z). The authors would like to thank Dr. S.J. Opella, Francesca Marassi, Michael Mesleh for many helpful discussions, Roberto Di Fonzo for encouragement and support, David Live and Beverly Ostrowski for help with NMR experiments. We also benefited from the facilities at the Minnesota High-Field NMR Center in the Department of Biochemistry, Molecular Biology, and Biophysics; University of Minnesota. NMR instrumentation was provided with funds from the NSF (BIR-961477) and the University of Minnesota Medical School. ",

year = "2004",

month = oct,

doi = "10.1016/j.chemphyslip.2004.09.018",

language = "English (US)",

volume = "132",

pages = "133--144",

journal = "Chemistry and Physics of Lipids",

issn = "0009-3084",

publisher = "Elsevier Ireland Ltd",

number = "1",

}

TY - JOUR

T1 - Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm

T2 - Application to phospholamban

AU - Mascioni, Alessandro

AU - Eggimann, Becky L.

AU - Veglia, Gianluigi

N1 - Funding Information: This work was supported in part by grants to G.V. (NIH GM64742; AHA 0160465Z). The authors would like to thank Dr. S.J. Opella, Francesca Marassi, Michael Mesleh for many helpful discussions, Roberto Di Fonzo for encouragement and support, David Live and Beverly Ostrowski for help with NMR experiments. We also benefited from the facilities at the Minnesota High-Field NMR Center in the Department of Biochemistry, Molecular Biology, and Biophysics; University of Minnesota. NMR instrumentation was provided with funds from the NSF (BIR-961477) and the University of Minnesota Medical School.

PY - 2004/10

Y1 - 2004/10

N2 - Dipolar waves are distinct hallmarks of both the secondary and tertiary structures of α-helical proteins that are immobilized in membrane bilayers or embedded in anisotropic media. We present a simple, semi-empirical approach that exploits the modulation of the amplitude and average of dipolar waves to determine the topology of α-helical proteins. Moreover, we describe the application of this method for the structural determination of a detergent solubilized membrane protein, phospholamban (PLB) that is involved in calcium regulation of cardiac muscle. When combined with high-resolution solid-state NMR data, this method can serve as a fast route for determining the topology of helical membrane proteins solubilized in detergent micelles.

AB - Dipolar waves are distinct hallmarks of both the secondary and tertiary structures of α-helical proteins that are immobilized in membrane bilayers or embedded in anisotropic media. We present a simple, semi-empirical approach that exploits the modulation of the amplitude and average of dipolar waves to determine the topology of α-helical proteins. Moreover, we describe the application of this method for the structural determination of a detergent solubilized membrane protein, phospholamban (PLB) that is involved in calcium regulation of cardiac muscle. When combined with high-resolution solid-state NMR data, this method can serve as a fast route for determining the topology of helical membrane proteins solubilized in detergent micelles.

KW - Ca-ATPase

KW - DPC micelles

KW - Dipolar waves

KW - Exhaustive search

KW - Helical wheels

KW - Membrane proteins

KW - NMR

KW - Phospholamban

KW - Polyacrylamide gel

KW - Residual dipolar couplings

KW - SERCA

KW - α-Helix

UR - http://www.scopus.com/inward/record.url?scp=7744243314&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=7744243314&partnerID=8YFLogxK

U2 - 10.1016/j.chemphyslip.2004.09.018

DO - 10.1016/j.chemphyslip.2004.09.018

M3 - Article

C2 - 15530454

AN - SCOPUS:7744243314

SN - 0009-3084

VL - 132

SP - 133

EP - 144

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

IS - 1

ER -

Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm: Application to phospholamban

Abstract

Bibliographical note

Keywords

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this