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J ‐based 2D homonuclear and heteronuclear correlation in solid‐state proteins
Author(s) -
Chen Lingling,
Kaiser J. Michael,
Lai Jinfeng,
Polenova Tatyana,
Yang Jun,
Rienstra Chad M.,
Mueller Leonard J.
Publication year - 2007
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.2107
Subject(s) - homonuclear molecule , heteronuclear molecule , chemistry , solid state nuclear magnetic resonance , solid state , two dimensional nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , computational chemistry , chemical physics , nuclear magnetic resonance spectroscopy , stereochemistry , molecule , organic chemistry , physics
Scalar‐based two‐dimensional heteronuclear experiments are reported for NCO and NCA chemical shift correlation in the solid state. In conjunction with homonuclear CACO correlation, these experiments form a useful set for tracing connectivities and assigning backbone resonances in solid‐state proteins. The applicability of this approach is demonstrated on two proteins, the β 1 immunoglobulin binding domain of protein G at 9.4 T and reassembled thioredoxin at 14.1 T, using different decoupling conditions and MAS frequencies. These constant‐time J ‐based correlation experiments exhibit increased resolution in the indirect dimension owing to homonuclear and heteronuclear decoupling, and because the indirect evolution and transfer periods are combined into a single constant time interval, this increased resolution is not obtained at the cost of sensitivity. These experiments are also shown to be compatible with in‐phase anti‐phase (IPAP) selection, giving increased resolution in the directly detected dimension. Copyright © 2007 John Wiley & Sons, Ltd.