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Many proteins bear sugar residues that modulate their functionality. Clues about the energy landscape and accessibility of sugar conformations in immunoglobulin G will contribute to an understanding of the mechanistic and energetic aspects of glycobiology and immunology.
The radical SAM superfamily of enzymes provides, yet again, fertile ground for the discovery of amazing new biochemical transformations. Strong evidence is now presented for an unprecedented radical fragmentation-recombination of L-tryptophan to a derivative that is incorporated into the complex antibiotic nosiheptide, highlighting the versatility of radical mechanisms for complex biochemical reactions.
Conformational transitions triggered by the binding of neurotransmitters open the gate of the ion channel domain of glutamate receptors, regulating the transmission of information through the nervous system. Using single-molecule fluorescence resonance energy transfer (smFRET), the agonist-binding domain of the GluA2 receptor, isolated in solution, is observed to interconvert among distinct large-scale conformational states.
Monoubiquitylation of histone H2B is found to disrupt condensation of chemically defined chromatin fibers. A novel fluorescence-based assay is used in concert with analytical ultracentrifugation to uncover the synergistic roles of histone acetylation and ubiquitylation on chromatin dynamics.
The vast majority of core structures of protein and peptide glycosylation motifs belong to either O-linked or N-linked glycans. A recent publication describes the structure and biosynthesis of an unusual S-linked glycan linkage in the antibacterial glycopeptide sublancin.
A new quantitative proteomic approach can identify reactive cysteine residues in native proteins and distinguish them on the basis of reactivity. This resource-rich study offers a useful new technology and is a significant step toward understanding the reactivity and functions of cysteines in cells.
The development of small-molecule probes for use in neural stem cells demonstrates the importance of endogenous ROS signaling in regulating in vivo phenotypes.
