Using a technique that illuminates subtle changes in individual proteins, chemistry researchers at Cornell University have uncovered new insight into the underlying causes of Amyotrophic Lateral Sclerosis (ALS). Brian Crane, professor of chemistry and chemical biology, led one study and co-authored a follow-up on a spectroscopic method that detects subtle changes to copper-containing proteins in solution. He and Jack Freed, professor of physical chemistry, have developed the method together with Petr Borbat, associate director of Cornell's National Biomedical Center for Advanced ESR Technology. The first study, which proved the principle of the technique -- pulsed dipolar electron spin resonance (ESR) spectroscopy -- was published Oct. 7 in Biophysical Journal; the second paper, which used the technique and others to connect ALS symptoms with protein aggregation was authored with collaborators from The Scripps Research Institute and appeared Oct. 14 in Proceedings of the National Academy of Sciences (PNAS). A complex neurodegenerative disease, ALS often has a genetic component -- genetic defects that cause it can be inherited. Scientists have long known that one of the culprit genes codes for the protein "superoxide dismutase 1" or SOD1 -- a critical copper-containing enzyme that protects cells against oxidative damage by destroying free radicals. … Continue reading
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