Journal of Biomolecular NMR

, Volume 67, Issue 4, pp 321–321 | Cite as

Erratum to: CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysis

  • Simon P. Skinner
  • Rasmus H. Fogh
  • Wayne Boucher
  • Timothy J. Ragan
  • Luca G. Mureddu
  • Geerten W. Vuister
Erratum

Erratum to: J Biomol NMR (2016) 66:111–124 DOI 10.1007/s10858-016-0060-y

The authors have become aware that the first introductory paragraph of Skinner et al. [J Biomol NMR (2016) 66:111–124, doi: 10.1007/s10858-016-0060-y] was plagiarized from the paper by Lee et al. [J Biomol NMR (2016) 64:307–332. doi: 10.1007/s10858-016-0029-x].

This was the result of an unfortunate and unintentional mistake in the first draft of the manuscript, prepared by the first author, which did not get corrected in the final submitted manuscript. The authors accept their shared responsibility for this error and apologize to Lee et al. for the unauthorized usage of their text. They wish to replace the paragraph with the following text:

Introduction

NMR spectroscopy is a vital, non-invasive, analytical technique with a broad range of applicability, including materials science, medical diagnosis, industrial process control, and chemistry (ur-Rahman and Choudhary 2015). It is also used in many fields of biomolecular research (Bertini et al. 2012), where it allows for the study of molecular systems at the atomic level under conditions similar to those in cellular systems, and even in cells themselves. NMR derives its power from its ability to measure a wide and diverse range of observables that can be suitably tailored to yield the relevant information (Vuister et al. 2011), yielding information on both structure and dynamics (Baldwin and Kay 2009; Anthis and Clore 2015). Together, this yields an exquisite picture of the molecular processes, with relevance to both normal and aberrant cellular functioning.

References

  1. Anthis NJ, Clore GM (2015) Visualizing transient dark states by NMR spectroscopy. Q Rev Biophys 48:35–116CrossRefGoogle Scholar
  2. Baldwin AJ, Kay LE (2009) NMR spectroscopy brings invisible protein states into focus. Nat Chem Biol 5:808–814CrossRefGoogle Scholar
  3. Bertini I, McGreevy KS, Parigi G (2012) NMR of biomolecules. Wiley, WeinheimCrossRefGoogle Scholar
  4. ur-Rahman A, Choudhary MI (2015) Applications of NMR spectroscopy, vol 1. Elsevier, AmsterdamCrossRefGoogle Scholar
  5. Vuister GW, Tjandra N, Shen Y et al (2011) Measurement of structural restraints. In: Roberts G, Lian L-Y (eds) Protein NMR spectroscopy: practical techniques and applications. Wiley, London, pp 83–157CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2017

Authors and Affiliations

  • Simon P. Skinner
    • 1
  • Rasmus H. Fogh
    • 1
  • Wayne Boucher
    • 2
  • Timothy J. Ragan
    • 1
  • Luca G. Mureddu
    • 1
  • Geerten W. Vuister
    • 1
  1. 1.Department of Molecular and Cell Biology, Leicester Institute for Structural- and Chemical BiologyUniversity of LeicesterLeicesterUK
  2. 2.Department of BiochemistryUniversity of CambridgeCambridgeUK

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