Based on the famous ""mfold"", the UNAFold software package is an integrated collection of programs that simulate nucleic acid folding and hybridization, and its melting pathways for one or two single-stranded molecules. The package predicts folding for single-stranded RNA or DNA through combination of free energy minimization, partition function calculations and stochastic sampling. For melting simulations, the package computes entire melting profiles, not just melting temperatures.
Interest in biomolecules including proteins and oligonucleotides has exploded in recent years, but while supplies of raw materials are relatively abundant, an ongoing problem encountered is separation andor purification of these materials. Displacement chromatography can be used to perform such difficult separations in an efficient and cost effective manner.
The creation of miniature biochemical analysis systems using microfavrication technology is a recent significant development in the field of micofluidics. These systems offer advantages such as size reduction, power reduction, and increased reliability. However, current systems are tailored to a specific task, and thus are unable to be reconfigured and reprogramed to handly a variety of tasks.
Displacement chromatography has attracted signifcant attention as a powerful technique for the purification of bioherapeutic proteins and oligunucleotides. Displacement chromatography enables simultaneous concentration and purification in a single step, which is significant in the purifcation of biopharmaceuticals. However, the major obstacle in implementing this technique is the lack of a sufficient diversity of appropriate displace candidates that are applicable across a wide spectrum of bioseparation demands.
This invention is directed to a high-throughput process for screening proteins for kinetic stability.Kinetically stable proteins are trapped in one conformation and have a high barrier to unfolding, so they are resistant to aggregation and degradation and have a longer half-life.The ability to quickly and easily identify kinetically stable proteins would have a myriad of applications in the biotechnology industry, pharmaceutical industry, and in basic life science research.
While there have been rapid advances in microscale device fabrication, microfluidics, and lab-on-a-chip technology, there is still a need to immobilize biomolecules (especially proteins) on a microfluidics apparatus, while maintaining high biological activity and electroosmotic flow (EOF) capability. This invention relates to the discovery that certain polymers containing both ionic and hydrophobic groups can be reproducibly adhered to microfluidic channels and can be used to simulataneously immobilize biocatalysts with good catalytic activity while supporting EOF.
Chemicals affect living organisms in both positive and negative ways, depending on the chemical. Chemicals can have different effects on different organisms, for example, potential drugs that work in animals studies but fail in human trials. A major reason to these differences is that species, individuals, and organs all have different kinds and amounts of enzymes. There is a need for a technology to rapidly, effectively, and economically test the heatlh effects of chemicals.
After discovering that a natural product has a particular, useful biological activity, it is desirable to prepare analogs of the natural product. However, natural products and their analogs are typically complex molecules requiring multi-step syntheses that are usually laborious, costly, and time consuming. This invention is directed to a microfluidics device that can be used to prepare natural products and their analogs.
This invention is directed to a step-wise enzymatic synthesis of combinatorial libraries of polymeric compounds prepared on a solid support in a configuration suitable for high-throughput screening for use in drug discovery and related fields. This invention provides compositions and methods for generating and screening libraries of phenolicanilinic polymers (and their related quinine forms) attached to a suitable surface and synthesized using enzymatic catalysis.
In process biotechnology, purification of proteins from complex biological mixtures involves a series of complicated recovery steps, each of which can compromise the purity and yield of the desired product. An advance in this area has been the introduction of self-cleaving protein linkers, achieved by combining binding domains with modified self-splicing protein elements known as inteins.