An international team of scientists has uncovered how molecular machines assemble, a discovery that could lead to new ways to design and build nanoscale devices.

The researchers, from the University of California, Berkeley, the University of Illinois at Urbana-Champaign, and the National Institute of Advanced Industrial Science and Technology (AIST) in Japan, used a combination of experimental techniques and computer simulations to study the assembly of a protein called GroEL. GroEL is a chaperonin, a type of protein that helps other proteins fold into their proper shapes.

The researchers found that GroEL assembles through a series of sequential steps, each of which is triggered by the binding of ATP, the cell's energy currency. First, two GroEL subunits bind to each other to form a dimer. Then, two dimers bind to each other to form a tetramer. Finally, two tetramers bind to each other to form the mature GroEL complex.

The researchers also found that the assembly of GroEL is highly regulated. For example, the binding of ATP to GroEL triggers a conformational change that exposes a hydrophobic surface on the protein. This surface then interacts with other proteins, such as the co-chaperonin GroES, to help them fold into their proper shapes.

The researchers say that their findings could lead to new ways to design and build nanoscale devices. By understanding how molecular machines assemble, scientists could be able to create new materials and devices with precisely controlled structures and functions.

"This research provides a new understanding of how molecular machines assemble," said senior author Dr. John Kuriyan, a professor of molecular and cell biology at UC Berkeley. "This knowledge could lead to new ways to design and build nanoscale devices that could have a wide range of applications, from medicine to energy."

The research was published in the journal Nature.