https://nova.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:31714 15N relaxation data demonstrate high flexibility of the polypeptide segment linking the C-peptide to the OB-domain and somewhat increased flexibility of the C-peptide compared with the OB-domain, suggesting that the C-peptide either retains high mobility in the bound state or is in a fast equilibrium with an unbound state.]]> Wed 11 Apr 2018 17:44:50 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:10610 Sat 24 Mar 2018 08:13:51 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:10449 Sat 24 Mar 2018 08:08:01 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:28373 Escherichia coli sliding clamp occurs via a sequential mechanism that involves two subsites (I and II). Here, we report the development of small-molecule inhibitors that mimic this mechanism. The compounds contain tetrahydrocarbazole moieties as "anchors" to occupy subsite I. Functional groups appended at the tetrahydrocarbazole nitrogen bind to a channel gated by the side chain of M362 and lie at the edge of subsite II. One derivative induced the formation of a new binding pocket, termed subsite III, by rearrangement of a loop adjacent to subsite I. Discovery of the extended binding area will guide further inhibitor development.]]> Sat 24 Mar 2018 07:35:58 AEDT ]]>