Imaging Membrane Protein Helical Wheels

J. Wang; J. Denny; C. Tian; S. Kim; Y. Mo; F. Kovacs; Z. Song; K. Nishimura; Z. Gan; R. Fu; J. R. Quine; T. A. Cross

doi:10.1006/jmre.2000.2037

Imaging Membrane Protein Helical Wheels

J. Wang, J. Denny, C. Tian, S. Kim, Y. Mo, F. Kovacs, Z. Song, K. Nishimura, Z. Gan, R. Fu, J. R. Quine, T. A. Cross

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

258 Scopus citations

Abstract

Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this α-helix. The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid specific labels around the "PISA wheel" defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained.

Original language	English (US)
Pages (from-to)	162-167
Number of pages	6
Journal	Journal of Magnetic Resonance
Volume	144
Issue number	1
DOIs	https://doi.org/10.1006/jmre.2000.2037
State	Published - May 2000
Externally published	Yes

Keywords

Membrane proteins
N solid-state NMR
Orientational constraints
Oriented samples
PISEMA

ASJC Scopus subject areas

Biophysics
Biochemistry
Nuclear and High Energy Physics
Condensed Matter Physics

Access to Document

10.1006/jmre.2000.2037

Cite this

@article{a43e579a0dab4f7cbfe8bae3b332bb27,

title = "Imaging Membrane Protein Helical Wheels",

abstract = "Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this α-helix. The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid specific labels around the {"}PISA wheel{"} defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained.",

keywords = "Membrane proteins, N solid-state NMR, Orientational constraints, Oriented samples, PISEMA",

author = "J. Wang and J. Denny and C. Tian and S. Kim and Y. Mo and F. Kovacs and Z. Song and K. Nishimura and Z. Gan and R. Fu and Quine, {J. R.} and Cross, {T. A.}",

note = "Funding Information: The authors are indebted to S. J. Opella and F. M. Marassi for sharing their manuscript with us prior to submission. The authors also thank the staff of the NHMFL NMR facility, in particular, A. Blue, as well as the staff of the Bioanalytical Synthesis and Services Laboratory, H. Henricks and U. Goli, for their expertise and maintenance of the instrumentation essential for this effort. This work was supported by the National Science Foundation, DMB 9603935 (T.A.C. and J.R.Q.) and DBI 9602233 (J.K.D.). The work was largely performed at the National High Magnetic Field Laboratory supported by NSF Cooperative Agreement (DMR-9527035) and the State of Florida.",

year = "2000",

month = may,

doi = "10.1006/jmre.2000.2037",

language = "English (US)",

volume = "144",

pages = "162--167",

journal = "Journal of Magnetic Resonance",

issn = "1090-7807",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Imaging Membrane Protein Helical Wheels

AU - Wang, J.

AU - Denny, J.

AU - Tian, C.

AU - Kim, S.

AU - Mo, Y.

AU - Kovacs, F.

AU - Song, Z.

AU - Nishimura, K.

AU - Gan, Z.

AU - Fu, R.

AU - Quine, J. R.

AU - Cross, T. A.

N1 - Funding Information: The authors are indebted to S. J. Opella and F. M. Marassi for sharing their manuscript with us prior to submission. The authors also thank the staff of the NHMFL NMR facility, in particular, A. Blue, as well as the staff of the Bioanalytical Synthesis and Services Laboratory, H. Henricks and U. Goli, for their expertise and maintenance of the instrumentation essential for this effort. This work was supported by the National Science Foundation, DMB 9603935 (T.A.C. and J.R.Q.) and DBI 9602233 (J.K.D.). The work was largely performed at the National High Magnetic Field Laboratory supported by NSF Cooperative Agreement (DMR-9527035) and the State of Florida.

PY - 2000/5

Y1 - 2000/5

N2 - Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this α-helix. The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid specific labels around the "PISA wheel" defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained.

AB - Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this α-helix. The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid specific labels around the "PISA wheel" defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained.

KW - Membrane proteins

KW - N solid-state NMR

KW - Orientational constraints

KW - Oriented samples

KW - PISEMA

UR - http://www.scopus.com/inward/record.url?scp=0034184852&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034184852&partnerID=8YFLogxK

U2 - 10.1006/jmre.2000.2037

DO - 10.1006/jmre.2000.2037

M3 - Editorial

C2 - 10783287

AN - SCOPUS:0034184852

VL - 144

SP - 162

EP - 167

JO - Journal of Magnetic Resonance

JF - Journal of Magnetic Resonance

SN - 1090-7807

IS - 1

ER -

Imaging Membrane Protein Helical Wheels

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this