NMR Spectroscopy On Large Proteins
Traditionally, nuclear magnetic resonance spectroscopy has been limited to relatively small proteins or protein domains. This is in part caused by problems resolving overlapping peaks in larger proteins, but this has been alleviated by the introduction of isotope labelling and multidimensional experiments. Another more serious problem is the fact that in large proteins the magnetization relaxes faster, which means there is less time to detect the signal. This in turn causes the peaks to become broader and weaker, and eventually disappear. Two techniques have been introduced to attenuate the relaxation: transverse relaxation optimized spectroscopy (TROSY) and deuteration of proteins. By using these techniques it has been possible to study proteins in complex with the 900 kDa chaperone GroES-GroEL.
Read more about this topic: Nuclear Magnetic Resonance Spectroscopy Of Proteins
Famous quotes containing the words large and/or proteins:
“... when you make it a moral necessity for the young to dabble in all the subjects that the books on the top shelf are written about, you kill two very large birds with one stone: you satisfy precious curiosities, and you make them believe that they know as much about life as people who really know something. If college boys are solemnly advised to listen to lectures on prostitution, they will listen; and who is to blame if some time, in a less moral moment, they profit by their information?”
—Katharine Fullerton Gerould (1879–1944)
“Civilization means food and literature all round. Beefsteaks and fiction magazines for all. First-class proteins for the body, fourth-class love-stories for the spirit.”
—Aldous Huxley (1894–1963)