Proteins perform the many functions of biological cells. This ability arises from the particular three-dimensional structure into which proteins fold at physiological temperature. The quick and precise folding of proteins depends on their molecular environment, e.g., water or lipid membrane, and is being investigated in many laboratories today. A new study from a computational - experimental collaboration investigated the folding and resulting structure of a protein, ubiquitin, in ethylene-glycol, commonly known as antifreeze, mixed with water. In this mixture the folding could be monitored at very low temperature in "slow motion" and resolved in great detail. Computational modeling using NAMD and VMD suggested that adding antifreeze to water leaves ubiquitin folding unaffected and this was born out indeed by further observation. Antifreeze is offering now a wider window into the study of the amazing abilities of other proteins.