Scientists have discovered more in the processes of protein folding

Biophysicists at the JILA Physics Research Center at the University of Colorado, USA, have more surprisingly measured the folding of proteins and are surprised to find that their folding processes are more complex than scientists have predicted. This means that our understanding on the degree of protein is still in the fur. Protein response is far more sophisticated than we have detected in the past 17 years. Thus, more research involved in recombinant mouse proteins should be done.

The basic composition of protein molecules is the amino acid chain. Through a series of intermediate processes, like the origami, the amino acid chain is folded into a three-dimensional structure, and then having a function. Accurately describing this folding process requires the formation of all intermediate states. The latest research reveals many unknown states in the process, and the results are published in the March 3 issue of the journal Science.

Researchers are researching a membrane protein that converts light into chemical energy, called bacteriorhodopsin (BR), with a molecular weight of about 26 kD. It provides a model for cell membrane receptor proteins and also contributes to elucidating the mechanism of interaction between the receptor and the signal in the signal transduction pathway of the human body, the BR or the proton protein of the ionomer channel on the cell membrane, and the role of the proton transfer membrane, so that it can be the other ion channel protein. Finally, its photoelectric response and photochromic specific make it have broad prospects in the solar cell, artificial retina, optical information storage, neural networks, bio-chip and other fields. Therefore, BR research has attracted the attention of countless scientists in the world. However, the folding of membrane proteins is more difficult than the folding of globular proteins with relatively small size.

Tom Perkins and colleagues who led the study used the nano-scale atomic force microscope (AFM) to stretch the BR protein and measure its degree of stretch at different stretching rates (nanometers per second). The measurement method comes from JILA's previous study, a soft AFM short probe (short, soft AFM) that can quickly measure the sudden change in force during protein development and immediately feed back a signal in the middle of the protein. By further refining these AFM probes, JILA researchers can detect BR proteins at different pull rates faster (faster than 100 times) and more accurate (10 times higher accuracy).

The JILA team found that the intermediate state was not only more than expected, and that the entire folding process was only 8 microseconds (1 microsecond equal to one millionth of a second). The results explain why there is a long-standing difference between experimental data and molecular simulations. At the same time, for the molecular simulation means to provide confidence in the future study of membrane protein behavior identified a path.

The technology can also be applied to many other molecular studies such as medical, protein, and drug interactions. More specific examples, such as structural and functional studies of proteins that are similar to BR structures are associated with many human diseases and drugs. By the way, Flarebio provides you with superior recombinant proteins such as recombinant ECE1 at competitive prices.