Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy

Zoltán Kóta; Tibor Páli; Neil Dixon; Terry P. Kee; Michael A. Harrison; John B.C. Findlay; Malcolm E. Finbow; Derek Marsh

doi:10.1021/bi7025112

Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy

Zoltán Kóta, Tibor Páli, Neil Dixon, Terry P. Kee, Michael A. Harrison, John B.C. Findlay, Malcolm E. Finbow, Derek Marsh

Glasgow Caledonian University

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

Abstract

Peptides were designed that are based on candidate transmembrane sequences of the Vo-sector from the vacuolar H+-ATPase of Saccharomyces cerevisiae. Spin-label EPR studies of lipid–protein interactions were used to characterize the state of oligomerization, and polarized IR spectroscopy was used to determine the secondary structure and orientation, of these peptides in lipid bilayer membranes. Peptides corresponding to the second and fourth transmembrane domains (TM2 and TM4) of proteolipid subunit c (Vma3p) and of the putative seventh transmembrane domain (TM7) of subunit a (Vph1p) are wholly, or predominantly, a-helical in membranes of dioleoyl phosphatidylcholine.

Original language	English
Pages (from-to)	3937-3949
Number of pages	13
Journal	Biochemistry
Volume	47
Issue number	12
DOIs	https://doi.org/10.1021/bi7025112
Publication status	Published - 1 Feb 2008

Keywords

biochemistry
transmembrane peptides
phospholipid membranes
ATPase

Documents and Links

10.1021/bi7025112

http://researchonline.gcu.ac.uk/sls/243

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Kóta, Zoltán ; Páli, Tibor ; Dixon, Neil ; Kee, Terry P. ; Harrison, Michael A. ; Findlay, John B.C. ; Finbow, Malcolm E. ; Marsh, Derek. / Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy. In: Biochemistry. 2008 ; Vol. 47, No. 12. pp. 3937-3949.

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title = "Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy",

abstract = "Peptides were designed that are based on candidate transmembrane sequences of the Vo-sector from the vacuolar H+-ATPase of Saccharomyces cerevisiae. Spin-label EPR studies of lipid–protein interactions were used to characterize the state of oligomerization, and polarized IR spectroscopy was used to determine the secondary structure and orientation, of these peptides in lipid bilayer membranes. Peptides corresponding to the second and fourth transmembrane domains (TM2 and TM4) of proteolipid subunit c (Vma3p) and of the putative seventh transmembrane domain (TM7) of subunit a (Vph1p) are wholly, or predominantly, a-helical in membranes of dioleoyl phosphatidylcholine.",

keywords = "biochemistry, transmembrane peptides, phospholipid membranes, ATPase",

author = "Zolt{\'a}n K{\'o}ta and Tibor P{\'a}li and Neil Dixon and Kee, {Terry P.} and Harrison, {Michael A.} and Findlay, {John B.C.} and Finbow, {Malcolm E.} and Derek Marsh",

note = "Originally published in: Biochemistry (2008), 47 (12), pp.3937–3949.",

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Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy. / Kóta, Zoltán; Páli, Tibor; Dixon, Neil; Kee, Terry P.; Harrison, Michael A.; Findlay, John B.C.; Finbow, Malcolm E.; Marsh, Derek.

In: Biochemistry, Vol. 47, No. 12, 01.02.2008, p. 3937-3949.

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

TY - JOUR

T1 - Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy

AU - Kóta, Zoltán

AU - Páli, Tibor

AU - Dixon, Neil

AU - Kee, Terry P.

AU - Harrison, Michael A.

AU - Findlay, John B.C.

AU - Finbow, Malcolm E.

AU - Marsh, Derek

N1 - Originally published in: Biochemistry (2008), 47 (12), pp.3937–3949.

PY - 2008/2/1

Y1 - 2008/2/1

N2 - Peptides were designed that are based on candidate transmembrane sequences of the Vo-sector from the vacuolar H+-ATPase of Saccharomyces cerevisiae. Spin-label EPR studies of lipid–protein interactions were used to characterize the state of oligomerization, and polarized IR spectroscopy was used to determine the secondary structure and orientation, of these peptides in lipid bilayer membranes. Peptides corresponding to the second and fourth transmembrane domains (TM2 and TM4) of proteolipid subunit c (Vma3p) and of the putative seventh transmembrane domain (TM7) of subunit a (Vph1p) are wholly, or predominantly, a-helical in membranes of dioleoyl phosphatidylcholine.

AB - Peptides were designed that are based on candidate transmembrane sequences of the Vo-sector from the vacuolar H+-ATPase of Saccharomyces cerevisiae. Spin-label EPR studies of lipid–protein interactions were used to characterize the state of oligomerization, and polarized IR spectroscopy was used to determine the secondary structure and orientation, of these peptides in lipid bilayer membranes. Peptides corresponding to the second and fourth transmembrane domains (TM2 and TM4) of proteolipid subunit c (Vma3p) and of the putative seventh transmembrane domain (TM7) of subunit a (Vph1p) are wholly, or predominantly, a-helical in membranes of dioleoyl phosphatidylcholine.

KW - biochemistry

KW - transmembrane peptides

KW - phospholipid membranes

KW - ATPase

U2 - 10.1021/bi7025112

DO - 10.1021/bi7025112

M3 - Article

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SP - 3937

EP - 3949

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

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