Scientists from Baylor College of Medicine (BCM) and Rice University have figured out how to look at and identify the protein structure. This breakthrough will help future scientists locate the active sites being used in cancer and other diseases. The information has been put online in the Proceedings of the National Academy of Science (PNAS). It uses math algorithms and X-ray crystallography. The math part of it defines all the positions the protein can flex or bend. X-ray crystallography "a technique in which protein crystals are bombarded with X-rays, producing a diffraction pattern that reveals the precise three-dimensional arrangement of every atom in the protein". The head researcher Jianpeng Ma expects this technique to help with a better understanding of supramolecular (more complex then a molecule) complexes that have limited information. William Lipscomb of Harvard University, one of the inventors of X-ray crystallography said the new successes involving this X-ray are phenomenal and that this technique of mapping out proteins has been the largest advancement in X-rays in two decades.
Since proteins are made out of strings of amino acids they tend to move a lot. But the part of the protein that moves the most is the part that plays the biggest role in the protein, for example, the place where an enzyme catalyzes a reaction. This is problem because the protein usually keeps moving and if you take an X-ray of a moving object it comes out fuzzy, so it is still a diffuculty to map out the vital part of the protein.
