Structural differences between the SH3-HOOK-GuK domains of SAP90/PSD-95 and SAP97

The SH3-HOOK-GUK domains of the postsynaptic scaffolding proteins SAP90/PSD-95 and SAP97 are established targets of synaptic plasticity processes in the brain. A crucial molecular mechanism involved is the transition of this domain to different conformational states. We purified the SH3-HOOK-GUK domain of both proteins to examine variations in protein conformation and stability. As monitored by circular dichroism and differential scanning calorimetry, SAP97 (T_m = 64 °C) is significantly more thermal stable than SAP90/PSD-95 (T_m = 52 °C) and follows a bimodal phase transition. GdmCl-induced equilibrium unfolding of both proteins follows the two-state transitions and thus does not involve the accumulation of stable intermediate state(s). Equilibrium unfolding of SAP97 is highly cooperative from a native state to an unfolded state. In contrast, SAP90/PSD-95 follows a non-cooperative transition from native to unfolded states. A highly cooperative unfolding reaction in case of SAP97 indicates that the protein existed initially as a compact, well-folded structure, while the gradual, non-cooperative melting reaction in case of SAP90/PSD-95 indicates that the protein is in comparison more flexible.     

Graphene-Based Plasmonic Sensor at THz Frequency with Photonic Spin Hall Effect Assisted by Magneto-optic Phenomenon

Plasmonics - Graphene monolayer of sub-nanometer thickness shows strong metallic and plasmonic behavior in terahertz (THz) frequency range. This plasmonic effect varies considerably when graphene...     

Minimum Norm Invariant Quadratic Estimation of a Covariance Matrix in Linear Model

A general linear model with a known covariance structure is considered. The method of Minimum Norm Quadratic estimation extending RAO'S (1972) argument is outlined. This method is illustrated for a particular model where it is noted that MINQE used for estimating intraclass correlation coefficient yields the maximum likelihood estimate.