Charu Chaudhry

TL;DR: In this paper, the authors demonstrate that the fusogenic structure is formed by the destabilization of hemagglutinin (HA) at neutral pH, with either heat or denaturant urea, triggering a conformational change that is biochemically indistinguishable from the change triggered by low pH.

TL;DR: It is demonstrated that the desensitized state of kainate receptors acts as a deep energy well offsetting the stabilizing effects of dimer interface mutants, and that the deactivation ofkainate receptor responses is dominated by entry into desensitization states.

TL;DR: Analytical ultracentrifugation is used to probe the energetic effects of allosteric ions on kainate receptor dimer stability in solution, using a GluR6 mutant that desensitizes slowly and indicates that ions can contribute substantial free energy to active state stabilization in both these receptors.

TL;DR: Results indicate that the native structure of HA is trapped in a metastable state and that the fusogenic conformation is released by destabilization of native structure, which could have implications for understanding the membrane-fusion step of HIV infection.

TL;DR: This work describes an approach of computationally accounting for signals from sedimenting buffer components through explicitly modeling their redistribution with Lamm equation solutions, implemented in the software SEDFIT.