Scientists searching for protein-protein interactions generally must look for them in vitro. But available techniques, such as chemical crosslinking and coimmunoprecipitation, are prone to false-positive and false-negative results. Cell lysis procedures, for instance, may bring into contact proteins that normally are compartmentalized in the cell, while wash procedures can dissociate fragile intermolecular interactions. And uncontrolled chemical methods can make even the most solitary polypeptide seem promiscuous.
Now, a team of researchers at the Max Planck Institute of Molecular Cell Biology and Genetics in Dresden, Germany, has created a new approach that may make detecting protein interactions easier, and more reliable in living mammalian cells.1
The new research builds on pioneering work at the Scripps Research Institute in San Diego, where Peter Schultz developed a method for modifying tRNAs to selectively incorporate non-natural amino acids into a single position within a protein. But Schultz's method is time consuming and requires extensive ...
