Patricia C. Weber

TL;DR: The HCV NS5B apoenzyme structure reported here can accommodate a template:primer duplex without global conformational changes, supporting the hypothesis that this structure is essentially preserved during the reaction pathway.

TL;DR: In this paper, a resolution structure of the HCV helicase from the positive-stranded RNA hepatitis C virus reveals a molecule with distinct NTPase and RNA binding domains, and the structure supports a mechanism of helicase activity involving initial recognition of the requisite 3' singlestranded region on the nucleic acid substrate by a conserved arginine-rich sequence on the RNA binding domain.

TL;DR: The high-resolution, refined structures of eNOS and iNOS reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer.

TL;DR: The scNS3-NS4A structure provides the first atomic view of polyprotein cis processing, and suggests autoinhibition and substrate-induced activation mechanisms for regulation of NS3 protease activity.

TL;DR: The efficacy of this technique for protein mapping was demonstrated by the mass spectral analyses of the peptide fragmentation of several biologically active proteins, including cytochrome c, ubiquitin, lysozyme, myoglobin, and interferon α‐2b.