The next generation of medicines will rely heavily upon our ability to quickly assess the structures and stabilities of protein-based biotherapeutics, including degradation products, engineered constructs, and antibody-antigen complexes. Such endeavours are both slow and challenging using standard biophysical tools. In this presentation, I discuss recent developments surrounding collision induced unfolding (CIU) methods that aim to bridge this technology gap. CIU uses ion mobility-mass spectrometry (IM-MS) to measure the stability and unfolding pathways of gas-phase proteins, without the need for covalent labels or tagging, and consuming 10-100 times less sample than almost any other label-free technology. Recent developments in high-throughput CIU screening methods, their ability to track alterations in biomolecular structure as a function of stress, and software developments that seek to enhance CIU information content will be discussed.