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Extending the Applicability of Exact Nuclear Overhauser Enhancements to Large Proteins and RNA
Author(s) -
Nichols Parker J.,
Born Alexandra,
Henen Morkos A.,
Strotz Dean,
Celestine Chi N.,
Güntert Peter,
Vögeli Beat
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800237
Subject(s) - nuclear overhauser effect , observable , millisecond , relaxation (psychology) , rna , physics , two dimensional nuclear magnetic resonance spectroscopy , statistical physics , chemistry , nuclear magnetic resonance spectroscopy , biological system , chemical physics , nuclear magnetic resonance , quantum mechanics , biology , biochemistry , gene , neuroscience
Distance‐dependent nuclear Overhauser enhancements (NOEs) are one of the most popular and important experimental restraints for calculating NMR structures. Despite this, they are mostly employed as semiquantitative upper distance bounds, and this discards the wealth of information that is encoded in the cross‐relaxation rate constant. Information that is lost includes exact distances between protons and dynamics that occur on the sub‐millisecond timescale. Our recently introduced exact measurement of the NOE (eNOE) requires little additional experimental effort relative to other NMR observables. So far, we have used eNOEs to calculate multistate ensembles of proteins up to approximately 150 residues. Here, we briefly revisit eNOE methodology and present two new directions for the use of eNOEs: applications to large proteins and RNA.