ChemBioChem

Cover image for Vol. 15 Issue 16

Editor: Peter Gölitz; Editorial Board Chairs: Thomas Carell, Donald Hilvert, Barbara Imperiali

Online ISSN: 1439-7633

Associated Title(s): ChemCatChem, ChemMedChem, ChemPhysChem, ChemSusChem

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November 17, 2014

Very Important Paper: Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR using Segmental Isotope Labeling

Tobias Schubeis, Torsten Lührs, Christiane Ritter*

Solid-state NMR has become a powerful technique for the elucidation of the structures of large protein complexes. However, spectral complexity and sensitivity remain serious challenges. Protein trans-splicing by the split intein DnaE from Nostoc punctiforme allows specific segments of a full-length protein to be isotopically labeled under a wide variety of conditions. Christiane Ritter (Helmholtz Centre for Infection Research, Germany) and co-workers have now employed this approach to obtain solid-state NMR spectra of a fungal prion protein (HET-s) with significantly improved spectral quality. Protein trans-splicing can be easily combined with other isotope labeling strategies to facilitate the resonance assignment and collection of structural restraints of proteins by solid-state NMR.

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Recently Published Articles

  1. Cotranscriptionally Folded RNA Nanostructures Pave the Way to Intracellular Nanofabrication

    Dr. Jiang Li, Dr. Jie Chao, Jiye Shi and Prof. Dr. Chunhai Fan

    Article first published online: 21 NOV 2014 | DOI: 10.1002/cbic.201402627

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    Go out on the tiles: Well-defined RNA architectures are readily assembled by cotranscriptional folding of single-stranded RNA tiles in an isothermal environment; this represents an important step toward intracellular fabrication of nanodevices for theranostic applications.

  2. Active Site Targeting of Hedgehog Precursor Protein with Phenylarsine Oxide

    Timothy S. Owen, Xie Jian Xie, Benjamin Laraway, Dr. George Ngoje, Prof. Chunyu Wang and Prof. Brian P. Callahan

    Article first published online: 21 NOV 2014 | DOI: 10.1002/cbic.201402421

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    Lost in maturation: Hedgehog proteins, whose signaling activities are linked to multiple human cancers, undergo a cholesterol-dependent autoprocessing event that is essential for bioactivity. The trivalent arsenical compound, phenylarsine oxide, was found to inhibit this reaction irreversibly.

  3. SUMO-Mimicking Peptides Inhibiting Protein SUMOylation

    Dr. Bo Zhao, Eric B. Villhauer, Karan Bhuripanyo, Prof. Dr. Hiroaki Kiyokawa, Prof. Dr. Hermann Schindelin and Prof. Dr. Jun Yin

    Article first published online: 20 NOV 2014 | DOI: 10.1002/cbic.201402472

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    SUMO goes small: Heptamer peptides were developed as compact versions of the 97-residue SUMO protein to block the SUMO activating enzyme (SAE) and SUMO conjugating enzyme (Ubc9) from transferring SUMO to its modification targets.

  4. Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95

    Dr. Jonas N. N. Eildal, Dr. Anders Bach, Dr. Jakob Dogan, Dr. Fei Ye, Prof. Mingjie Zhang, Dr. Per Jemth and Prof. Kristian Strømgaard

    Article first published online: 18 NOV 2014 | DOI: 10.1002/cbic.201402547

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    The tandem PDZ1-2 domain of PSD-95 is a structurally important module and a promising novel drug target. Here, conformationally restricted dimeric inhibitors of PSD-95 were designed, synthesized, and subsequently examined by fluorescence polarization, isothermal titration calorimetry, protein NMR, and stopped-flow kinetics. This provided insight into the molecular details of dynamic dimeric ligand/tandem PDZ domain interaction.

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    Dr. Subhash R. Rauthu, Tze Chieh Shiao, Priv.-Doz.Dr. Sabine André, Dr. Michelle C. Miller, Élodie Madej, Prof. Kevin H. Mayo, Prof. Hans-Joachim Gabius and Prof. René Roy

    Article first published online: 18 NOV 2014 | DOI: 10.1002/cbic.201402474

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    Screening small libraries of glycomimetics: Evaluation of biorelevant cell assays of families of aglycone-modified Lac and LacNAc derivatives followed by HSQC NMR can select candidates with finely tuned selectivities and protein “hot spots”.

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