Learn Biophysical Chemistry with Upadhyay and Upadhyay PDF 29

mutated utrophin, a homolog of dystrophin, is structurally related to dystrophin but it has a normal c-terminal domain and a shorter n-terminal domain in comparison to dystrophin. it is fully functional to restore the sarcolemma stability by forming its complex with dystrophin. mutations in dystrophin lead to a truncated dystrophin that is associated with only the c-terminal domain and forms truncated utrophin. these two proteins are very similar and functionally redundant.

upadhyay and upadhyay biophysical chemistry pdf 29

muscular dystrophy patients with the most severe cases have no utrophin and only retain the c-terminal domain of dystrophin. the studies of this project aim at better understanding the structural causes and phenotypic consequences of these mutations.

for dystrophin, mutations in these small structural domains can also cause the disease, and structural information at the atomic level is lacking. the questions that we wish to answer are the following: what are the structures of the c-terminal domains and how do they interact with dystrophin? what are the effects of mutations on the protein structures? can we develop therapeutic treatments against muscular dystrophy by finding out the defective mechanisms and structures of the disease-causing mutations?

kohyun kang received his b.s. (1997) and ph.d. (2002) degrees from the department of mechanical and biomedical engineering, the university of minnesota, minneapolis, mn, usa, where he is now a junior faculty member. his research focuses on the novel applications of nanotechnology for smart drug delivery and cellular imaging. since joining the faculty of the bioengineering department at seoul national university in 2013, dr. kang has pursued experimental and theoretical research topics that include electrical recording across the brain tissues, cell migration, and electrophysiology.