Abstract: Compounds and methods for refolding of proteins in an aqueous solution. In particular, biocompatible multiblock copolymer surfactants such as poloxamers, meroxapols, poloxamines, or polyols are used to catalyze proper refolding without changing the protein composition, and restore the protein to its native conformation and native biological function. The methods can be practiced both in vivo and in vitro. The biocompatible multiblock copolymer surfactants can be used for renaturation of recombinantly expressed proteins, and for renaturation of proteins that are unfolded due to heat, irradiation, mechanical shearing, electrical shock, frostbite, chemical stress, and other abiotic or biotic stresses.

Abstract: Compounds and methods for refolding of proteins in an aqueous solution. In particular, biocompatible multiblock copolymer surfactants such as poloxamers, meroxapols, poloxamines, or polyols are used to catalyze proper refolding without changing the protein composition, and restore the protein to its native conformation and native biological function. The methods can be practiced both in vivo and in vitro. The biocompatible multiblock copolymer surfactants can be used for renaturation of recombinantly expressed proteins, and for renaturation of proteins that are unfolded due to heat, irradiation, mechanical shearing, electrical shock, frostbite, chemical stress, and other abiotic or biotic stresses.

Abstract: Compounds and methods for refolding of proteins in an aqueous solution. In particular, biocompatible multiblock copolymer surfactants such as poloxamers, meroxapols, poloxamines, or polyols are used to catalyze proper refolding without changing the protein composition, and restore the protein to its native conformation and native biological function. The methods can be practiced both in vivo and in vitro. The biocompatible multiblock copolymer surfactants can be used for renaturation of recombinantly expressed proteins, and for renaturation of proteins that are unfolded due to heat, irradiation, mechanical shearing, electrical shock, frostbite, chemical stress, and other abiotic or biotic stresses.

Abstract: Disclosed herein is a magnetic resonance imaging calibration assembly in particular, for dynamic contrast—enhanced magnetic resonance imaging. An exemplary magnetic resonance imaging calibration assembly according to the present disclosure can comprise a subject receptacle for receiving at least a portion of a subject. The exemplary magnetic resonance imaging calibration assembly can further comprise a plurality of phantom compartments, each of which can contain a calibration phantom with a predetermined known T relaxation time. The plurality of phantom compartments can be attached to the subject receptacle in different ways. For example, according to some exemplary embodiments of the 10 present invention, the phantom compartments are separate compartments attached or fixed onto the subject receptacle. According to other exemplary embodiments, the phantom compartments can be formed at least partially by the subject receptacle. The phantom can be for a T1 calibration making use of its known T1.

Abstract: A new, clinically applicable magnetic resonance imaging (MRI) method has been developed for in vivo imaging of a population of cells in a subject based on a class of paramagnetic divalent vanadyl-based contrast agents. The method includes administering to a subject a VO2+-based contrast agent and monitoring distribution of the VO2+-based contrast agent in the subject using magnetic resonance imaging.

Abstract: Compounds and methods for refolding of proteins in an aqueous solution. In particular, biocompatible multiblock copolymer surfactants such as poloxamers, meroxapols, poloxamines, or polyols are used to catalyze proper refolding without changing the protein composition, and restore the protein to its native conformation and native biological function. The methods can be practiced both in vivo and in vitro. The biocompatible multiblock copolymer surfactants can be used for renaturation of recombinantly expressed proteins, and for renaturation of proteins that are unfolded due to heat, irradiation, mechanical shearing, electrical shock, frostbite, chemical stress, and other abiotic or biotic stresses.