Single Molecule RNA Base Identification with a Biological Nanopore

Supplement to the F.M.S Government Gazette, September 10, 1914

Sequence of abductin, the molluscan ‘rubber’ protein

Traduction française du roman moyen-anglais Of Arthour and of Merlin tiré du manuscrit Auchinleck (Adv MS 19.2.1) de la National Library of Scotland. Traduction annotée des vers 2503-270

Prolonging assembly through dissociation:A self assembly paradigm in microtubules

We study a one-dimensional model of microtubule assembly/disassembly in which GTP bound to tubulins within the microtubule undergoes stochastic hydrolysis. In contrast to models that only consider a cap of GTP-bound tubulin, stochastic hydrolysis allows GTP-bound tubulin remnants to exist within the microtubule. We find that these buried GTP remnants enable an alternative mechanism of recovery from shrinkage, and enhances fluctuations of filament lengths. Under conditions for which this alternative mechanism dominates, an increasing depolymerization rate leads to a decrease in dissociation rate and thus a net increase in assembly.Comment: accepted for publication in Physical Review

Methods of enhancing translocation of charged analytes through transmembrane protein pores

The patent refers to the field of 'peptides'. The invention relates to enhancing translocation of a charged analyte through a transmembrane protein pore. Translocation is enhanced by increasing the net opposing charge of the barrel or channel and/or entrance of the pore. The invention also relates to pores enhanced in accordance with the invention

Stochastic Sensing of Nanomolar Inositol 1,4,5-Trisphosphate with an Engineered Pore

AbstractThe introduction of a ring of arginine residues near the constriction in the transmembrane β barrel of the staphylococcal α-hemolysin heptamer yielded a pore that could be almost completely blocked by phosphate anions at pH 7.5. Block did not occur with other oxyanions, including nitrate, sulfate, perchlorate, and citrate. Based on this finding, additional pores were engineered with high affinities for important cell signaling molecules, such as the Ca2+-mobilizing second messenger inositol 1,4,5-trisphosphate (IP3), that contain phosphate groups. One of these engineered pores, PRR-2, provides a ring of fourteen arginines that project into the lumen of the transmembrane barrel. Remarkably, PRR-2 bound IP3 with low nanomolar affinity while failing to bind another second messenger, adenosine 3′, 5′-cyclic monophosphate (cAMP). The engineered α-hemolysin pores may be useful as components of stochastic sensors for cell signaling molecules