Very-long-distance correlations in proteins revealed by solid-state NMR spectroscopy

Bingwen Hu; Julien Trébosc; Oliver Lafon; Qun Chen; Yuichi Masuda; K. Takegoshi; Jean Paul Amoureux

doi:10.1002/cphc.201200548

Very-long-distance correlations in proteins revealed by solid-state NMR spectroscopy

Bingwen Hu^*, Julien Trébosc, Oliver Lafon, Qun Chen, Yuichi Masuda, K. Takegoshi, Jean Paul Amoureux

^*Corresponding author for this work

School of Physics and Electronic Science

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

22 Scopus citations

Abstract

I still see you: A new pulse sequence, SHA+, little sensitive to dipolar truncation, allows direct or relayed polarization transfer between ¹³C atoms, distant by 3.5-9.6 Å, in amyloid fibrils (see picture). SHA+ can also be used in a broadband way with the weak rf-condition of v₁v_R≈0.2-0.3 which permits the investigation of temperature-sensitive biological systems.

Original language	English
Pages (from-to)	3585-3588
Number of pages	4
Journal	ChemPhysChem
Volume	13
Issue number	16
DOIs	https://doi.org/10.1002/cphc.201200548
State	Published - 12 Nov 2012

Keywords

Amyloid beta-peptides
NMR spectroscopy
magic-angle spinning
polarization transfer
protein structures

Access to Document

10.1002/cphc.201200548

Cite this

@article{43d764871b284fa69c79f5e99d8c1022,

title = "Very-long-distance correlations in proteins revealed by solid-state NMR spectroscopy",

abstract = "I still see you: A new pulse sequence, SHA+, little sensitive to dipolar truncation, allows direct or relayed polarization transfer between 13C atoms, distant by 3.5-9.6 {\AA}, in amyloid fibrils (see picture). SHA+ can also be used in a broadband way with the weak rf-condition of v1vR≈0.2-0.3 which permits the investigation of temperature-sensitive biological systems.",

keywords = "Amyloid beta-peptides, NMR spectroscopy, magic-angle spinning, polarization transfer, protein structures",

author = "Bingwen Hu and Julien Tr{\'e}bosc and Oliver Lafon and Qun Chen and Yuichi Masuda and K. Takegoshi and Amoureux, \{Jean Paul\}",

year = "2012",

month = nov,

day = "12",

doi = "10.1002/cphc.201200548",

language = "英语",

volume = "13",

pages = "3585--3588",

journal = "ChemPhysChem",

issn = "1439-4235",

publisher = "Wiley-VCH Verlag",

number = "16",

}

TY - JOUR

T1 - Very-long-distance correlations in proteins revealed by solid-state NMR spectroscopy

AU - Hu, Bingwen

AU - Trébosc, Julien

AU - Lafon, Oliver

AU - Chen, Qun

AU - Masuda, Yuichi

AU - Takegoshi, K.

AU - Amoureux, Jean Paul

PY - 2012/11/12

Y1 - 2012/11/12

N2 - I still see you: A new pulse sequence, SHA+, little sensitive to dipolar truncation, allows direct or relayed polarization transfer between 13C atoms, distant by 3.5-9.6 Å, in amyloid fibrils (see picture). SHA+ can also be used in a broadband way with the weak rf-condition of v1vR≈0.2-0.3 which permits the investigation of temperature-sensitive biological systems.

AB - I still see you: A new pulse sequence, SHA+, little sensitive to dipolar truncation, allows direct or relayed polarization transfer between 13C atoms, distant by 3.5-9.6 Å, in amyloid fibrils (see picture). SHA+ can also be used in a broadband way with the weak rf-condition of v1vR≈0.2-0.3 which permits the investigation of temperature-sensitive biological systems.

KW - Amyloid beta-peptides

KW - NMR spectroscopy

KW - magic-angle spinning

KW - polarization transfer

KW - protein structures

UR - https://www.scopus.com/pages/publications/84868533464

U2 - 10.1002/cphc.201200548

DO - 10.1002/cphc.201200548

M3 - 文章

C2 - 22890906

AN - SCOPUS:84868533464

SN - 1439-4235

VL - 13

SP - 3585

EP - 3588

JO - ChemPhysChem

JF - ChemPhysChem

IS - 16

ER -

Very-long-distance correlations in proteins revealed by solid-state NMR spectroscopy

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this