Literature DB >> 10527751

Dual processing of two-dimensional exchange data in magic angle spinning NMR of solids.

R Tycko1, A E Berger.   

Abstract

We discuss procedures for processing data in rotor-synchronized two-dimensional magic angle spinning (2D MAS) NMR exchange measurements for both structural and dynamical studies. We show, both mathematically and experimentally, that there are two distinct data processing procedures that lead to 2D MAS exchange spectra with purely absorptive crosspeaks. One procedure is that described previously by Hagemeyer, Schmidt-Rohr, and Spiess (HSS). The other procedure is related, but different, and leads to crosspeak intensities given by the formulae of Herzfeld, Roberts, and Griffin (HRG). In 2D MAS exchange experiments on doubly (13)C-labeled l-alanylglycylglycine, we demonstrate that the HSS and HRG crosspeak intensities can be extracted separately from the same data set and contain independent information. Processing and analysis of 2D MAS exchange data with both the HSS and the HRG procedures may enhance utilization of the information content of 2D MAS exchange measurements.

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Year:  1999        PMID: 10527751     DOI: 10.1006/jmre.1999.1877

Source DB:  PubMed          Journal:  J Magn Reson        ISSN: 1090-7807            Impact factor:   2.229


  6 in total

1.  Analysis of local conformation of membrane-bound and polycrystalline peptides by two-dimensional slow-spinning rotor-synchronized MAS exchange spectroscopy.

Authors:  Charles M Gabrys; Jun Yang; David P Weliky
Journal:  J Biomol NMR       Date:  2003-05       Impact factor: 2.835

2.  Probing site-specific conformational distributions in protein folding with solid-state NMR.

Authors:  Robert H Havlin; Robert Tycko
Journal:  Proc Natl Acad Sci U S A       Date:  2005-02-17       Impact factor: 11.205

Review 3.  What can solid state NMR contribute to our understanding of protein folding?

Authors:  Kan-Nian Hu; Robert Tycko
Journal:  Biophys Chem       Date:  2010-05-23       Impact factor: 2.352

4.  The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218-289): a solid-state NMR study.

Authors:  Chandrakala Gowda; Giorgia Zandomeneghi; Herbert Zimmermann; Anne K Schütz; Anja Böckmann; Matthias Ernst; Beat H Meier
Journal:  J Biomol NMR       Date:  2017-11-01       Impact factor: 2.835

5.  Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMR.

Authors:  Oleg N Antzutkin; John J Balbach; Robert Tycko
Journal:  Biophys J       Date:  2003-05       Impact factor: 4.033

6.  Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.

Authors:  Kan-Nian Hu; Robert H Havlin; Wai-Ming Yau; Robert Tycko
Journal:  J Mol Biol       Date:  2009-07-30       Impact factor: 5.469

  6 in total

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