PubMed · 14152860
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
P DE SOMER. 1964-05-16. [INTERFERON].. https://pubmed.ncbi.nlm.nih.gov/14152860/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Monolayers of DNA chains of polymeric dimensions, considered here to be longer than approximately 100 nucleotides, are widely encountered in biomolecular diagnostics as well as present for a model system for investigating behavior of polyelectrolytes at interfaces. A major challenge in advancing such applications is assembling the DNA on the surface in a controlled way. Although covalent immobilization is expected to produce optimal stability, the multitude of potential reactive sites along the contour of long DNA molecules requires that any chemical transformations be strictly site-specific to preserve control over attachment geometry and function. A synthetic approach to fabricating monolayers of DNA genes on gold using polymeric anchor (adhesion) films is presented that (i) possesses stringent site-specificity of surface-attachment, (ii) exhibits excellent stability to elevated temperatures, allowing denaturation of duplex chains at 90 degrees C without loss of surface-linked strands, and (iii) achieves surface coverages suitable for investigating multichain polyelectrolyte behavior in regimes of strong interchain interactions.
Many hairpin loops are expanded versions of smaller, stable ones. Herein we investigate the extent to which the energetics and structure of d(cGNAg) hairpin loops will tolerate sequence variation. Changing the closing base pair from CG to GC was found to completely eliminate loop-loop interactions; in contrast, expanding the loop at the 3'-end resulted in similar energetics and nonadditivity parameters as the parent loop, suggesting that loop-loop interactions remain intact and highly coupled upon expansion. Together, these data suggest that the CG closing base pair forms an essential platform upon which a stable d(GNA) hairpin loop can fold and that this loop can undergo 3'-expansion with little effect to its structure or energetics.
Selected isoflavones (genistein, daidzein, formononetin, prunetin, biochanin A, and two synthetic isoflavones) were allowed to interact with soy and whey proteins. The reaction products were analyzed in terms of covalent binding at the nucleophilic side chains of proteins. Changes in molecular properties of the proteins derivatives were documented by SDS-PAGE, IEF, and SELDI-TOF-MS. The structural changes induced were studied using circular dichroism. The in vitro digestibility was assessed with trypsin. The results show that the occurrence of the catechol moiety, that is, the two adjacent (ortho) aromatic hydroxyl groups on ring B of the flavonoid structural skeleton appears to be prerequisite condition for covalent binding to proteins. The catechol moiety on ring A was less reactive. Its absence lead to a slight or no significant reaction, although noncovalent interactions may still be possible, even when lacking this structural element. A comparison of the data is also made with quercetin representing the flavonols.