Propensity for local folding induced by the urea fragment in short-chain oligomers.

Mixed oligomer formation between human alphaA-crystallin and its cataract-causing G98R mutant: structural, stability and functional differences.

Mutation of the glycine 98 residue to arginine in alphaA-crystallin has been shown to cause presenile cataract in an Indian family. Our earlier study showed that the mutant protein exhibits folding defects that lead to aggregation and inclusion body formation in Escherichia coli. Despite the presence of a normal copy, the pathology is seen in the heterozygous individuals. Formation of mixed oli...

Preparation and unique circular dichroism phenomena of urea-functionalized self-folding resorcinarenes bearing chiral termini through asymmetric hydrogen-bonding belts.

Chiral macrocycles with eight (R)- and (S)-methylbenzylurea residues on the resorcinarene skeleton linked through a hexyl or dodecyl spacer having amide linkages have been prepared by the reactions of the corresponding octaamine derivative with (R)- and (S)-alpha-methylbenzylisocyanate, respectively. In chloroform, the urea-functionalized resorcinarenes with hexyl spacers form intramolecular hy...

Application of Oligomers with Urea Linkage as Flame Retardant and Antibacterial Materials in Jute Fabric

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization

It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...

Aqueous urea solution destabilizes A 16–22 oligomers

We use long multiple trajectories generated by molecular dynamics simulations to probe the stability of oligomers of A 16–22 (KLVFFAE) peptides in aqueous urea solution. High concentration of urea promotes the formation of -strand structures in A 16–22 monomers, whereas in water they adopt largely compact random coil structures. The tripeptide system, which forms stable antiparallel -sheet stru...