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Turning proteins into hydrophobic floatable materials with multiple potential applications.

08:00 EDT 4th July 2019 | BioPortfolio

Summary of "Turning proteins into hydrophobic floatable materials with multiple potential applications."

Protein hydrogels are water-rich structure of cross-linked protein networks. The preparation of dry gels is conceptually simple. However, reports on innovative use of dry protein hydrogels are scarce, possibly because water removal would diminish intended properties. Here, an oil-like thiol-organosilane is proposed as a protein hydrogel-promoting agent that mediates the formation of hydrophobic composite gel networks with promising properties upon drying.

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Journal Details

This article was published in the following journal.

Name: Journal of colloid and interface science
ISSN: 1095-7103
Pages: 166-176

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Medical and Biotech [MESH] Definitions

Locomotor behavior not involving a steering reaction, but in which there may be a turning random in direction. It includes orthokinesis, the rate of movement and klinokinesis, the amount of turning, which are related to the intensity of stimulation.

A homodimerization protein interaction domain occurring at the N terminus of proteins that contain multiple copies of either CYS2-HIS2 ZINC FINGERS or KELCH REPEATS. It is characterized by a tightly intertwined dimer with an extensive hydrophobic interface. A surface-exposed groove lined with conserved amino acids is formed at the dimer interface, suggesting a peptide-binding site. Many BTB proteins are transcriptional regulators that are thought to regulate CHROMATIN structure.

Applies to movements of the forearm in turning the palm backward or downward or when applied to the foot, a combination of eversion and abduction movements in the tarsal and metatarsal joints, (turning the foot up and in toward the midline of the body).

A diverse family of extracellular proteins that bind to small hydrophobic molecules. They were originally characterized as transport proteins, however they may have additional roles such as taking part in the formation of macromolecular complexes with other proteins and binding to CELL SURFACE RECEPTORS.

Intracellular proteins that reversibly bind hydrophobic ligands including: saturated and unsaturated FATTY ACIDS; EICOSANOIDS; and RETINOIDS. They are considered a highly conserved and ubiquitously expressed family of proteins that may play a role in the metabolism of LIPIDS.

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