ChemBioChem

Cover image for Vol. 13 Issue 3

Editor: Peter Gölitz

Online ISSN: 1439-7633

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

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amino acids · antibiotics · antitumor agents · biocatalysis · bioinorganic chemistry · biosynthesis · carbohydrates · click chemistry · DNA · enzyme catalysis · enzymes · fluorescence · fluorescent probes · glycopeptides · hydrolases · inhibitors · medicinal chemistry · membranes · microarrays · natural products · NMR spectroscopy · peptides · peptidomimetics · photochemistry · polyketides · post-translational modifications · protein design · proteins · proteomics · RNA

Recently Published Articles

  1. Stereospecific Formation of a Ternary Complex of (S)-α,β-Fluoromethylene-dATP with DNA Pol β

    Brian T. Chamberlain, Dr. Vinod K. Batra, Dr. William A. Beard, Anastasia P. Kadina, David D. Shock, Dr. Boris A. Kashemirov, Dr. Charles E. McKenna, Dr. Myron F. Goodman and Dr. Samuel H. Wilson

    Article first published online: 7 FEB 2012 | DOI: 10.1002/cbic.201100738

    Thumbnail image of graphical abstract

    The influence of water: Crystallization of (R/S)-α,β-CHF-dATP with the preorganized pol β-DNA complex shows that (S)-α,β-CHF-dATP is preferentially bound to the active site with the C[BOND]F fluorine proximal to a structural water bound to Asp276.

  2. KlenTaq DNA Polymerase Adopts Unique Recognition States when Encountering Matched, Mismatched, and Abasic Template Sites: An NMR Study

    Bastian Holzberger, M. Gabriele Pszolla, Prof. Dr. Andreas Marx and Dr. Heiko M. Möller

    Article first published online: 7 FEB 2012 | DOI: 10.1002/cbic.201100802

    Thumbnail image of graphical abstract

    On the tracks of a DNA polymerase: NMR provides insights into DNA synthesis in a virtually label-free manner and under close-to-physiological conditions. Through the monitoring of the chemical-shift changes of multiple 13C-methyl methionine residues we found unique recognition states for canonical and noncanonical cases, thus indicating enzymatic cycling through distinct paths.

  3. Covalent Tagging of Phosphorylated Peptides by Phosphate-Specific Deoxyribozymes

    Dr. Amit Sachdeva, Dr. Madhavaiah Chandra, Jagadeeswaran Chandrasekar and Prof. Scott K. Silverman

    Article first published online: 7 FEB 2012 | DOI: 10.1002/cbic.201200048

    Thumbnail image of graphical abstract

    Hold your P's: Phosphorylated tyrosine and serine residues in peptides have been modified selectively by DNA catalysts (see graphic). These deoxyribozymes catalyze covalent attachment of an RNA tag to a range of peptide sequences, thus a proof of principle for a new approach to phosphopeptide analysis is established.

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