1,356 research outputs found

    Realization of the Space of Conformal Blocks in Lie Algebra Modules

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    AbstractUsing integrable irreducible representations of generalized twisted affine Lie algebra modules, we give a realization of the space of conformal blocks of conformal field theory on a stable algebraic curve. Many basic properties of the conformal blocks, such as finite dimensionality of the space, invariance of the conformal blocks under suitable formal neighborhood changes, and the property of ā€œpropagation of vacuaā€ are discussed. Finally, a relative local 1-form around a fixed point of the order two automorphism of the curve is given

    Voltage-dependent Gating Rearrangements in the Intracellular T1ā€“T1 Interface of a K+ Channel

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    The intracellular tetramerization domain (T1) of most eukaryotic voltage-gated potassium channels (Kv channels) exists as a ā€œhanging gondolaā€ below the transmembrane regions that directly control activation gating via the electromechanical coupling between the S4 voltage sensor and the main S6 gate. However, much less is known about the putative contribution of the T1 domain to Kv channel gating. This possibility is mechanistically intriguing because the T1ā€“S1 linker connects the T1 domain to the voltage-sensing domain. Previously, we demonstrated that thiol-specific reagents inhibit Kv4.1 channels by reacting in a state-dependent manner with native Zn2+ site thiolate groups in the T1ā€“T1 interface; therefore, we concluded that the T1ā€“T1 interface is functionally active and not protected by Zn2+ (Wang, G., M. Shahidullah, C.A. Rocha, C. Strang, P.J. Pfaffinger, and M. Covarrubias. 2005. J. Gen. Physiol. 126:55ā€“69). Here, we co-expressed Kv4.1 channels and auxiliary subunits (KChIP-1 and DPPX-S) to investigate the state and voltage dependence of the accessibility of MTSET to the three interfacial cysteines in the T1 domain. The results showed that the average MTSET modification rate constant (kMTSET) is dramatically enhanced in the activated state relative to the resting and inactivated states (āˆ¼260- and āˆ¼47-fold, respectively). Crucially, under three separate conditions that produce distinct activation profiles, kMTSET is steeply voltage dependent in a manner that is precisely correlated with the peak conductanceā€“voltage relations. These observations strongly suggest that Kv4 channel gating is tightly coupled to voltage-dependent accessibility changes of native T1 cysteines in the intersubunit Zn2+ site. Furthermore, cross-linking of cysteine pairs across the T1ā€“T1 interface induced substantial inhibition of the channel, which supports the functionally dynamic role of T1 in channel gating. Therefore, we conclude that the complex voltage-dependent gating rearrangements of eukaryotic Kv channels are not limited to the membrane-spanning core but must include the intracellular T1ā€“T1 interface. Oxidative stress in excitable tissues may perturb this interface to modulate Kv4 channel function

    Time-Varying Discrete-Time Wavelet Transforms

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