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The folded-sheet silica mesoporous material (FSM) having nanometer-size pores inside was filled with a high amount of functional membrane protein complex, namely the photosynthetic light-harvesting complex LH2 to capture the light energy. The LH2 complex in the FSM shows higher heat stability and higher circular symmetry of the absorption band of bacteriocholorophylls, which can be useful for the construction of new probes and reaction systems.

Circular dichroism (CD) and fluorescence spectroscopy are used to investigate the molecular details of the interaction in islet amyloid polypeptide (IAPP) with lipid membranes of varying composition. The potential roles of IAPP-membrane interaction and the novel membrane-bound alpha-helical conformation in IAPP aggregation are discussed.

The article discusses the synthesis, as well as the characterization of CHOBIMALT, a cholesterol-based detergent. The detergent is shown to highly enhance the thermal stability of hum an kappa opioid receptor type 1 on being added to the classical detergent micelles.

Controllable membrane formation is developed by making a subtle change at the molecular level. The photmanipulation of mesoscopic membrane structures in a noncontact and reversible manner has helped in understanding the mechanism of membrane self-organization and might be used is microreactors and drug-delivery systems.

The article discusses the development of a new bright monomeric photoactivabale red fluorescent protein, which can be employed for the two-color super-resolution of single particle tracking PALM of live cells. The protein is shown to exhibit better brightness and stability, as compared to the other monomeric proteins.

The new copper-selective fluorescent probes FluTPA1 and FluTPA2 are described, in which the tetradentate ligand tris[(2-pyridyl)methyl]amine (TPA) is connected to a reduced form of a fluorescein platform through a benzyl ether linkage. Confocal images of live cells have shown that FluTPA2 is membrane-permeable and has allowed visualization of [Cu.sup.I] present in living cells.

The replacement of Ala178 with Arg in the E-F loop of proteorhodopsin (PR), an archaeal-type rhodopsin in marine bacteria which shifts the [[lambda].sub.max] from 525 to 545 nm at neutral pH was examined to understand the molecular mechanism of the unusual mutation effect on color tuning. The results provide insight into unique structure of E-F loop in PR and the observed changes in color and p[K.sub.a] due to the mutation of Ala178 that disrupted the structure in the transmembrane region.

A study related to the effect of incorporation of a proton transporter, cytochrome c oxidase, into a membrane on the protonation kinetics of a fluorescent pH-sensitive probe attached at the surface of the protein is presented. The results indicated that the membrane plays a significant role to accelerate proton uptake by the membrane-bound proton transporter.

A site-directed fluorescence labeling technique is used to study the membrane-bound closed channel structure of helices of 4 and 5 (Lys-406-Asp-446) of the colicin E1 channel domain. The data revealed that both helices 4 and 5 are two separate amphipathic [alpha]-helices that are positioned parallel to the membrane surface.

A new gel system is described that has weakly aligned a molecule for solution NMR spectroscopy. The collagen gel has provided a robust and cost-effective alternative to align large biomolecules and membrane proteins in a magnetic field.

The use of phage display for identifying novel disulfide-constrained peptides capable of blocking the interaction between glycoprotein Ib[alpha] (GPIb[alpha]) and A1 domain of von Willebrand factor (vWF-A1) is described. These peptides are used for obtaining costructure information to support the development of small-molecule GPIb[alpha] antagonists.

A new method is developed for improving the resolution in the [super 15]N dimension of 1D [super 15]N and 2D [super 1]H - [super 15]N separated local field (SLF) experiments for oriented membrane protein systems. The resolution enhancement is necessary for assignment and structural exploitation of spectra for large oriented membrane proteins.

The issue of how the molecular organization of rod outer segments (ROS) discs might affect the timing of the photoresponse is addressed by explicitly simulating a patch of disc membrane in which the classical and the recent frameworks are compared by using mesoscopic Monte Carlo (MMC) simulations. An unexpected favorable effect on the temporal response of early phototransduction reactions can occur if high-density rhodopsin packing on ROS discs is characterized by a highly ordered structured organization rather than unspecific aggregation.

A second family of minimally cationic miniature proteins is created that has effectively crossed the plasma membrane of eukaryotic cells. The scaffolds are capable of supporting high affinity and specificity interactions in vitro and in vivo and hence the additional encoding of cellular permeability has expanded their utility.

The scanning of bilayer over the surface of an SDS-PAGE gel has enabled the direct detection membrane proteins from gels using single-channel recording. Hydrogen scanning with water-in-oil droplet bilayers has provided a new method for discovering and characterizing ion channels with the potential for high-throughput screening.

The aggregation number and shape of micelles formed by nine detergents commonly used in the study of membrane proteins are analyzed. The results have described the determinants of micelle formation and are used as a starting point to correlate detergent properties with detergent-protein interactions.

Report is presented on the microscopic, residue-specific evaluation of CERMAD stability in the Ezrin N/C complex obtained using hydrogen-deuterium exchange (HX) NMR experiments. The results illustrate the dynamic nature of the regulatory interface and provide a foundation for investigating the role of regulatory signals on the stability of this interface.

The simulation and detection algorithms are developed for various modes of biologically relevant complex diffusive phenomena, including confined and convective diffusion, and diffusion in the presence of barriers, rafts and interparticle interactions. Few examples are illustrated to show the use of conventional vs. the new computational methods in detecting these membrane phenomena.

The thiol-directed method has overcome most of the limitations present in other alignment media with polytopic helical membrane proteins and has provided a robust method for simple, stable alignments. Protein alignment through lanthanide metals is very important for the application of residual dipolar couplings (RDCs) to solve the NMR structures of polytopic helical membrane proteins.

Imaging of membrane proteins on cells using a cyano-labelled surface enhanced raman scattering (SERS) probe is described. It is seen that the strongest SERS signals originate from aggregates oriented in the appropriate direction with respect to the incident laser polarization and observed SERS hot-sites correlate well with small aggregated NPs.

The analysis of dipolar waves provides a significant step toward structure determination of helical membrane proteins by NMR spectroscopy. Dipolar waves are a representation of the mapping of protein structure onto NMR spectra through the anisotropic nuclear spin interactions in aligned samples.