The Graduate Center (GC) of the City University of New York (CUNY) has entered into a joint endeavor with Princeton University to explore the interface between biology and physics through the establishment of the Center for the Physics of Biological Function.
The experimental validation of an efficient iterative technique for compensating known position errors in a spherical near to far-field transformation (NTFFT) for elongated antennas using a minimum number of near-field (NF) measurements has been provided. This transformation exploits a non-redundant sampling representation of the voltage detected by the probe obtained by modeling a long antenna with a prolate ellipsoid.
New oral anticoagulants (NOACs) represent direct-acting drugs functioning selectively for one specific clotting factor. Their clinical indications are the prophylaxis and treatment of deep venous thrombosis and pulmonary embolism, the prevention of atherothrombotic episodes of individuals with acute coronary syndromes and atrial fibrillation
Peptoids, N-substituted glycine oligomers, are an important class of foldamers that can adopt polyproline type helices (PP-I and PP-II), given that the majority of their sequence consists of chiral bulky side chains. Herein we introduce a new approach for the stabilization of a pure PP-I-like peptoid helix via metal coordination. We performed a systematic spectroscopic study on a series of peptoid heptamers baring two 8-hydroxyquinoline ligands at fixed positions, and a mixture of chiral phenyl and alkyl substituents in varied positions along the peptoid backbone. We found that when the phenyl groups are located at the 3rd and 4th positions, the peptoid (7P6) gives upon Cu2+ binding a CD signal similar to that of a PP-I helix. Exciton couplet CD and EPR spectroscopies, as well as modifications to the length of 7P6 and acetylation provided insights into the unique folding of 7P6 via Cu binding, showing that it is led by two competing driving forces - coordination geometry and sequence.