Structural analysis of protein interfaces from 13C direct-detected paramagnetic relaxation enhancements

Tobias Madl; Isabella C. Felli; Ivano Bertini; Michael Sattler

doi:10.1021/ja1014508

Structural analysis of protein interfaces from ¹³C direct-detected paramagnetic relaxation enhancements

Tobias Madl, Isabella C. Felli, Ivano Bertini, Michael Sattler

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Abstract

The measurement of ¹³C 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 ¹³C direct-detected experiments. The ¹³C 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.

Original language	English
Pages (from-to)	7285-7287
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	132
Issue number	21
DOIs	https://doi.org/10.1021/ja1014508
State	Published - 2 Jun 2010

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title = "Structural analysis of protein interfaces from 13C direct-detected paramagnetic relaxation enhancements",

abstract = "The measurement of 13C 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 13C direct-detected experiments. The 13C 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.",

author = "Tobias Madl and Felli, {Isabella C.} and Ivano Bertini and Michael Sattler",

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T1 - Structural analysis of protein interfaces from 13C direct-detected paramagnetic relaxation enhancements

AU - Madl, Tobias

AU - Felli, Isabella C.

AU - Bertini, Ivano

AU - Sattler, Michael

PY - 2010/6/2

Y1 - 2010/6/2

N2 - The measurement of 13C 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 13C direct-detected experiments. The 13C 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.

AB - The measurement of 13C 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 13C direct-detected experiments. The 13C 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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U2 - 10.1021/ja1014508

DO - 10.1021/ja1014508

M3 - Article

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AN - SCOPUS:77952869538

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

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ER -

Structural analysis of protein interfaces from ¹³C direct-detected paramagnetic relaxation enhancements

Abstract

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