[CITATION][C] Structural explanation for the deficiency of S α1-antitrypsin
PR Elliott, PE Stein, D Bilton, RW Carrell… - Nature structural …, 1996 - nature.com
Untitled Page 1 Page 2 © 1996 Nature Publishing Group http://www.nature.com/nsmb and S
antitrypsin. The identical results from TUG gels of native M and of S at-antitrypsin indicate that
any inherent difference in molecular stability between the two is minor. This is supported by
findings of similar folding and unfolding transitions in guanidine hydrochloride and equivalent
transition of M and S at-antitrypsin to the latent (reactive loop stably inserted into the A P-sheet)
conformation on incubation at 67 ac in 0.7 M citratet2• N; compared to the severe Z-mutation …
antitrypsin. The identical results from TUG gels of native M and of S at-antitrypsin indicate that
any inherent difference in molecular stability between the two is minor. This is supported by
findings of similar folding and unfolding transitions in guanidine hydrochloride and equivalent
transition of M and S at-antitrypsin to the latent (reactive loop stably inserted into the A P-sheet)
conformation on incubation at 67 ac in 0.7 M citratet2• N; compared to the severe Z-mutation …