[HTML][HTML] A thermostable mutation located at the hydrophobic core of α1-antitrypsin suppresses the folding defect of the Z-type variant
J Kim, KN Lee, GS Yi, MH Yu - Journal of Biological Chemistry, 1995 - ASBMB
A thermostable mutation, F51L, at the hydrophobic core of human α 1-antitrypsin (α 1 AT)
increased the conformational stability of the molecule by decreasing the unfolding rate
significantly without altering the refolding rate. The mutation specifically influenced the
transition between the native state and a compact intermediate, which retained∼ 70% of the
far-UV CD signal, but which had most of the fluorescence signal already dequenched. The
mutant α 1 AT protein was more resistant than the wild-type protein to the insertion of the …
increased the conformational stability of the molecule by decreasing the unfolding rate
significantly without altering the refolding rate. The mutation specifically influenced the
transition between the native state and a compact intermediate, which retained∼ 70% of the
far-UV CD signal, but which had most of the fluorescence signal already dequenched. The
mutant α 1 AT protein was more resistant than the wild-type protein to the insertion of the …
