vpu Transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching

Andreas Kukol; Isaiah T. Arkin

doi:10.1016/S0006-3495(99)77007-4

vpu Transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching

Andreas Kukol
, Isaiah T. Arkin

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

84 Citations (Scopus)

Abstract

The recently developed method of site-directed Fourier transform infrared dichroism for obtaining orientational constraints of oriented polymers is applied here to the transmembrane domain of the vpu protein from the human immunodeficiency virus type 1 (HIV-1). The infrared spectra of the 31-residue-long vpu peptide reconstituted in lipid vesicles reveal a predominantly α-helical structure. The infrared dichroism data of the ¹³C- labeled peptide yielded a helix tilt β = (6.5 ± 1.7)°from the membrane normal. The rotational pitch angle ω, defined as zero for a residue located in the direction of the helix tilt, is ω = (283 ± 11)°for the ¹³C labels Val¹³/Val²⁰ and ω = (23 ± 11)°for the ¹³C labels Ala¹⁴/Val²¹. A global molecular dynamics search protocol restraining the helix tilt to the experimental value was performed for oligomers of four, five, and six subunits. From 288 structures for each oligomer, a left-handed pentameric coiled coil was obtained, which best fits the experimental data. The structure reveals a pore occluded by Trp residues at the intracellular end of the transmembrane domain.
Copyright © 1999 by the Biophysical Society

Original language	English
Pages (from-to)	1594-1601
Journal	Biophysical Journal
Volume	77
Issue number	3
DOIs	https://doi.org/10.1016/S0006-3495(99)77007-4
Publication status	Published - Sept 1999
Externally published	Yes

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Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].

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@article{bc89818e702b4c758b89c7e78acb4cd9,

title = "vpu Transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching",

abstract = "The recently developed method of site-directed Fourier transform infrared dichroism for obtaining orientational constraints of oriented polymers is applied here to the transmembrane domain of the vpu protein from the human immunodeficiency virus type 1 (HIV-1). The infrared spectra of the 31-residue-long vpu peptide reconstituted in lipid vesicles reveal a predominantly α-helical structure. The infrared dichroism data of the 13C- labeled peptide yielded a helix tilt β = (6.5 ± 1.7)°from the membrane normal. The rotational pitch angle ω, defined as zero for a residue located in the direction of the helix tilt, is ω = (283 ± 11)°for the 13C labels Val13/Val20 and ω = (23 ± 11)°for the 13C labels Ala14/Val21. A global molecular dynamics search protocol restraining the helix tilt to the experimental value was performed for oligomers of four, five, and six subunits. From 288 structures for each oligomer, a left-handed pentameric coiled coil was obtained, which best fits the experimental data. The structure reveals a pore occluded by Trp residues at the intracellular end of the transmembrane domain. Copyright {\textcopyright} 1999 by the Biophysical Society",

author = "Andreas Kukol and Arkin, \{Isaiah T.\}",

note = "Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].",

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doi = "10.1016/S0006-3495(99)77007-4",

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T1 - vpu Transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching

AU - Kukol, Andreas

AU - Arkin, Isaiah T.

N1 - Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].

PY - 1999/9

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N2 - The recently developed method of site-directed Fourier transform infrared dichroism for obtaining orientational constraints of oriented polymers is applied here to the transmembrane domain of the vpu protein from the human immunodeficiency virus type 1 (HIV-1). The infrared spectra of the 31-residue-long vpu peptide reconstituted in lipid vesicles reveal a predominantly α-helical structure. The infrared dichroism data of the 13C- labeled peptide yielded a helix tilt β = (6.5 ± 1.7)°from the membrane normal. The rotational pitch angle ω, defined as zero for a residue located in the direction of the helix tilt, is ω = (283 ± 11)°for the 13C labels Val13/Val20 and ω = (23 ± 11)°for the 13C labels Ala14/Val21. A global molecular dynamics search protocol restraining the helix tilt to the experimental value was performed for oligomers of four, five, and six subunits. From 288 structures for each oligomer, a left-handed pentameric coiled coil was obtained, which best fits the experimental data. The structure reveals a pore occluded by Trp residues at the intracellular end of the transmembrane domain. Copyright © 1999 by the Biophysical Society

AB - The recently developed method of site-directed Fourier transform infrared dichroism for obtaining orientational constraints of oriented polymers is applied here to the transmembrane domain of the vpu protein from the human immunodeficiency virus type 1 (HIV-1). The infrared spectra of the 31-residue-long vpu peptide reconstituted in lipid vesicles reveal a predominantly α-helical structure. The infrared dichroism data of the 13C- labeled peptide yielded a helix tilt β = (6.5 ± 1.7)°from the membrane normal. The rotational pitch angle ω, defined as zero for a residue located in the direction of the helix tilt, is ω = (283 ± 11)°for the 13C labels Val13/Val20 and ω = (23 ± 11)°for the 13C labels Ala14/Val21. A global molecular dynamics search protocol restraining the helix tilt to the experimental value was performed for oligomers of four, five, and six subunits. From 288 structures for each oligomer, a left-handed pentameric coiled coil was obtained, which best fits the experimental data. The structure reveals a pore occluded by Trp residues at the intracellular end of the transmembrane domain. Copyright © 1999 by the Biophysical Society

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U2 - 10.1016/S0006-3495(99)77007-4

DO - 10.1016/S0006-3495(99)77007-4

M3 - RGC 21 - Publication in refereed journal

C2 - 10465770

SN - 0006-3495

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JO - Biophysical Journal

JF - Biophysical Journal

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ER -

vpu Transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching

Abstract

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