Surprisingly, the mutant conjugate was also taken up into the cells in a similar pattern, albeit to a lesser degree. Both conjugates showed no cytotoxicity.

These conjugates show potential

for future use in magnetic resonance imaging studies of brain tumors after systemic or intraoperative local application.

The cytoplasm specificity of the conjugates also makes it a potential building block for the design of future cytoplasm-directed Immunology & Inflammation inhibitor imaging and therapeutic conjugates.”
“The spontaneous dissociation of six small ligands from the active site of FKBP (the FK506 binding protein) is investigated by explicit water molecular dynamics simulations and network analysis. The ligands have between four (dimethylsulphoxide) and eleven

(5-diethylamino-2-pentanone) non-hydrogen atoms, and an affinity for FKBP ranging from 20 to 0.2 mM. The conformations of the FKBP/ligand complex saved along multiple trajectories (50 runs at 310 K for each ligand) are grouped according to a set of intermolecular distances into nodes of a network, and the direct transitions between them are the links. The network analysis reveals that the bound state consists of several subbasins, i.e., binding modes characterized by distinct intermolecular hydrogen bonds and hydrophobic contacts. The dissociation kinetics show a simple (i.e., single-exponential) time dependence because the unbinding barrier is much higher than the barriers between subbasins in the bound state. The

unbinding transition state is made up of heterogeneous positions PFTα mw and orientations of the ligand in the FKBP active site, which correspond to multiple pathways of dissociation. For the six small ligands of FKBP, the weaker the binding affinity the closer to the bound state (along the intermolecular distance) are the transition state structures, which is a new manifestation of Hammond behavior. Experimental approaches to the study of fragment binding to proteins have limitations in temporal and spatial resolution. Our network analysis of the unbinding simulations of small inhibitors from an enzyme paints a clear picture of the free energy landscape (both thermodynamics and kinetics) of ligand unbinding.”
“Electron selleck compound spin-spin interaction in an asymmetric coupled quantum well (CQW) was investigated through electron spin-precession measurements. Precession (Larmor) frequencies from electrons localized in two CQWs were measured by means of polarization-and time-resolved photoluminescence measurements under a high magnetic field. At a low excitation power density, the Larmor frequency of the CQW was same as that of a single quantum well. The Larmor frequency of electron spin in one well was shifted to that in the other well as the excitation power density was increased. These experimental results are quantitatively explained by an exchange interaction between electrons localized in the two wells. (C) 2011 American Institute of Physics. [doi:10.1063/1.