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

Chair of Biomolecular NMR-Spectroscopy

Helmholtz Zentrum München German Research Center for Environmental Health
Technical University of Munich
University of Florence

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

31 Scopus citations

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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10.1021/ja1014508

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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.

UR - https://www.scopus.com/pages/publications/77952869538

U2 - 10.1021/ja1014508

DO - 10.1021/ja1014508

M3 - Article

C2 - 20462243

AN - SCOPUS:77952869538

SN - 0002-7863

VL - 132

SP - 7285

EP - 7287

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 21

ER -

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

Abstract

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