Silicon Mitigates Drought Stress in Wheat (Triticum aestivum L.) Through Improving Photosynthetic Pigments,Biochemical and Yield Characters

Silicon - Feeling prone to stress differs with plant production stage, water scarcity near commencement of grain filling phase has a significant reduced grain yield through fewer endosperm and sink...     

Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel

Staphylococcal alpha-hemolysin is a water soluble, monomeric, bacterial exotoxin, which forms heptameric pores in membranes. The rate determining step in assembly is the conversion of a heptameric prepore to the fully assembled pore in which the central glycine-rich domain of each subunit inserts into the membrane to form a 14 strand beta barrel. Barrel formation is accompanied by a conformational change in which each N terminus latches onto an adjacent subunit. In the monomer in solution, the central domain is loosely organized and exposed to solvent. In this study, 25 amino acids of the central domain were removed and replaced with the sequence Asp-Gly, which favors the formation of a type I' beta-turn, to yield a mutant devoid of hemolytic activity. Within minutes after synthesis in the absence of membranes, the mutant polypeptide spontaneously assembled into heptamers, as demonstrated by atomic force microscopy. Limited proteolysis suggested that the N termini of the subunits in the heptamers were in the fully assembled pore conformation rather than the prepore conformation. Based on these findings, the deletion is proposed to constrain the central domain and thereby force the creation of a shortened beta barrel, which in turn induces the additional structural changes that normally accompany pore formation. The truncated pore might make a useful framework for the construction of designed membrane active macromolecules.      

Far infrared spectrum of methylamine

The far-infrared (FIR) spectrum of CH₃NH₂ has been studied in the 25–125 cm^?1 region at a resolution of 0.005 cm^?1 with a BOMEM Fourier transform spectrometer. All of the^rR branches with K rotational quantum number from 5 to 13 have been identified for A-a and E-a torsion-inversion symmetries in the ground torsional state, as well as some branches of A-s and E-s symmetries and some in excited torsional states. The observed branches have been fitted to series expansions in order to determine the branch origins.     

Heptameric structures of two alpha-hemolysin mutants imaged with in situ atomic force microscopy

Atomic force microscopy has been used to study self-assembled structures of two alpha-hemolysin mutants. For a mutant (alphaHL-H5) that was locked into the prepore state on fluid phase egg-PC membranes, we visualized, for the first time, heptameric prepores and showed that the 7-fold axis in the prepore lies perpendicular to the membrane surface. For another mutant (TCM) with the transmembrane domain, the self-assembled oligomer that assumes the conformation of the fully assembled pore is also a heptamer. These results show that heptamers are the preferred oligomerization state of alpha-hemolysin.