Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening

Thomas Vosegaard; Kresten Bertelsen; Jan M. Pedersen; Lea Thøgersen; Birgit Schiøtt; Emad Tajkhorshid; Troels Skrydstrup; Niels Chr Nielsen

doi:10.1021/ja8000612

Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening

Thomas Vosegaard, Kresten Bertelsen, Jan M. Pedersen, Lea Thøgersen, Birgit Schiøtt, Emad Tajkhorshid, Troels Skrydstrup, Niels Chr Nielsen

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

Abstract

We demonstrate that a significant improvement in the spectral resolution may be achieved in solid-state NMR experiments of proteins in inhomogeneously disordered oriented lipid bilayers. Using ¹H homonuclear decoupling instead of standard ¹H heteronuclear decoupling, the ¹⁵N line widths may be reduced by up to seven times for such samples. For large oriented membrane proteins, such resolution enhancements may be crucial for assignment and structural interpretation.

Original language	English (US)
Pages (from-to)	5028-5029
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	130
Issue number	15
DOIs	https://doi.org/10.1021/ja8000612
State	Published - Apr 16 2008

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

Online availability

10.1021/ja8000612

Library availability

Discover UIUC Full Text

Cite this

@article{a8c349a9330946e48d29a31f56bc1d2a,

title = "Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening",

abstract = "We demonstrate that a significant improvement in the spectral resolution may be achieved in solid-state NMR experiments of proteins in inhomogeneously disordered oriented lipid bilayers. Using 1H homonuclear decoupling instead of standard 1H heteronuclear decoupling, the 15N line widths may be reduced by up to seven times for such samples. For large oriented membrane proteins, such resolution enhancements may be crucial for assignment and structural interpretation.",

author = "Thomas Vosegaard and Kresten Bertelsen and Pedersen, {Jan M.} and Lea Th{\o}gersen and Birgit Schi{\o}tt and Emad Tajkhorshid and Troels Skrydstrup and Nielsen, {Niels Chr}",

year = "2008",

month = apr,

day = "16",

doi = "10.1021/ja8000612",

language = "English (US)",

volume = "130",

pages = "5028--5029",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "15",

}

TY - JOUR

T1 - Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening

AU - Vosegaard, Thomas

AU - Bertelsen, Kresten

AU - Pedersen, Jan M.

AU - Thøgersen, Lea

AU - Schiøtt, Birgit

AU - Tajkhorshid, Emad

AU - Skrydstrup, Troels

AU - Nielsen, Niels Chr

PY - 2008/4/16

Y1 - 2008/4/16

N2 - We demonstrate that a significant improvement in the spectral resolution may be achieved in solid-state NMR experiments of proteins in inhomogeneously disordered oriented lipid bilayers. Using 1H homonuclear decoupling instead of standard 1H heteronuclear decoupling, the 15N line widths may be reduced by up to seven times for such samples. For large oriented membrane proteins, such resolution enhancements may be crucial for assignment and structural interpretation.

AB - We demonstrate that a significant improvement in the spectral resolution may be achieved in solid-state NMR experiments of proteins in inhomogeneously disordered oriented lipid bilayers. Using 1H homonuclear decoupling instead of standard 1H heteronuclear decoupling, the 15N line widths may be reduced by up to seven times for such samples. For large oriented membrane proteins, such resolution enhancements may be crucial for assignment and structural interpretation.

UR - http://www.scopus.com/inward/record.url?scp=42149124280&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=42149124280&partnerID=8YFLogxK

U2 - 10.1021/ja8000612

DO - 10.1021/ja8000612

M3 - Article

C2 - 18341279

AN - SCOPUS:42149124280

SN - 0002-7863

VL - 130

SP - 5028

EP - 5029

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 15

ER -

Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening

Abstract

ASJC Scopus subject areas

Online availability

Library availability

Related links

Fingerprint

Cite this