The measurement of C-13 directed-detected paramagnetic relaxation enhancements (PREs) on spin-labeled proteins combines the efficacy of PREs for the detection of long-range distance information with the favorable sensitivity and resolution of C-13 direct-detected experiments. The C-13 PREs provide long-range distance restraints to map binding interfaces in proteins and protein complexes and are especially useful for studies of high-molecular weight perdeuterated molecules.
Structural analysis of protein interfaces from 13C direct-detected paramagnetic relaxation enhancements / T.Madl; I.C.Felli; I.Bertini; M.Sattler. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 132 (21):(2010), pp. 7285-7287. [10.1021/ja1014508]
Structural analysis of protein interfaces from 13C direct-detected paramagnetic relaxation enhancements
FELLI, ISABELLA CATERINA;BERTINI, IVANO;
2010
Abstract
The measurement of C-13 directed-detected paramagnetic relaxation enhancements (PREs) on spin-labeled proteins combines the efficacy of PREs for the detection of long-range distance information with the favorable sensitivity and resolution of C-13 direct-detected experiments. The C-13 PREs provide long-range distance restraints to map binding interfaces in proteins and protein complexes and are especially useful for studies of high-molecular weight perdeuterated molecules.
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