Conformational isomers of denatured-unfolded proteins are rich in numbers and varied in shapes. They represent an opulent resource of biological molecules that have remained unexploited. The major obstacle in utilizing this untapped potential is that it is inherently difficult to isolate and characterize pure conformational isomers, not only because of the excessive large number, but also because of their instability and rapid inter-conversion. Our lab has developed a method for trapping selected conformational isomers of denatured proteins that are amenable to isolation, characterization and further applications. The method has potential usefulness, ranging from the comprehensive structural characterization of denatured proteins, to the elucidation of pathways of protein unfolding-folding, to the production of unlimited structurally defined non-native protein isomers for biomedical applications.