The three-dimensional structure of PrP110-136, a peptide encompassing the conserved hydrophobic region of the human prion protein, has been determined at high resolution in dodecylphosphocholine micelles by NMR. The results support the conclusion that the (Ctm)PrP, a transmembrane form of the prion protein, adopts a different conformation than the reported structures of the normal prion protein...

A series of catechol derivatives with a different number of linear alkyl chain substituents, and different length, have been shown to polymerize in the presence of aqueous ammonia and air, yielding hydrophobic coatings that present the ability to provide robust and efficient water repellency on weaved textiles, including hydrophilic cotton. The polymerization strategy presented exemplifies an a...

Cellulose dissolution and regeneration is an increasingly active research field due to the direct relevance for numerous production processes and applications. The problem is not trivial since cellulose solvents are of remarkably different nature and thus the understanding of the subtle balance between the different interactions involved becomes difficult but crucial. There is a current discuss...

DNA nanotechnology excels at rationally designing bottom-up structures that can functionally replicate naturally occurring proteins. Here we describe the design and generation of a stable DNA-based nanopore that structurally mimics the amphiphilic nature of protein pores and inserts into bilayers to support a steady transmembrane flow of ions. The pore carries an outer hydrophobic belt comprise...

The crystal structure of an 8-mer (S)-GNA duplex is presented. As a tool for phasing, the anomalous diffraction of two copper(II) ions within two artificial metallo-base pairs was employed. The duplex structure confirms a canonical Watson-Crick base pairing scheme of GNA with antiparallel strands. The duplex secondary structure is distinct from canonical A- and B-form nucleic acids and can be d...

Recent experiments suggest that the folding of certain proteins can take place entirely within a chaperonin-like cavity. These substrate proteins experience folding rate enhancements without undergoing multiple rounds of ATP-induced binding and release from the chaperonin. Rather, they undergo only a single binding event, followed by sequestration into the chaperonin cage. The present work uses...

Hydrophobic molecules are by definition difficult to hydrate. Previous studies in the area of hydrophobic hydration have therefore often relied on using amphiphilic where hydrophilic part a...