The spatial structure of amyloidogenic SEM1(68-107) peptide
We obtained the problems with overlap signals of SEM1(68-107) caused by high mobility of disordered fragments. The structure of SEM1(68-107) was determined by combining the results obtained for the peptide fragments (SEM1(68-85) and SEM1(86-107)).
structures with the least restraint violations
Schwieters, Kuszewski, Tjandra and Clore
semenogelin 1, amyloid fibril of human semen, HIV enhancer, PROTEIN FIBRIL