Volume 8 Issue 8, August 2001

Recent crystal structures suggest models for how an asymmetric E2/E2-like protein complex synthesizes a polyubiquitin chain that functions in DNA repair and NF-κB activation pathways.

The membrane-inserted structure of a synthetic fusion peptide of influenza virus hemagglutinin has been determined. Structures such as this will further our understanding of the roles of the fusion peptide and may provide a means to develop a systematic view for how fusion peptide mutations in hemagglutinin affect the membrane fusion process.

DNA polymerases play a central role in maintenance of genetic information, and the structures of polymerases in complex with DNA and dNTP provide valuable insights into mechanisms utilized by DNA polymerases to achieve high fidelity. Comparison of several high resolution complexes of DNA polymerases bound with relevant substrates indicates that the two major families of polymerases function by very similar mechanisms.

NMR experiments with partially aligned protein molecules in strongly denaturing conditions suggest that the unfolded state is less chaotic than is widely believed. Hence protein folding is probably less paradoxical than Levinthal originally thought.