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Title 

Folding pathway of human α₁-antitrypsin: characterization of an intermediate that is active but prone to aggregation

Authors 

Daeyou KimMyeong Hee Yu

Publisher 

Elsevier

Issue Date 

1996

Citation 

Biochemical and Biophysical Research Communications, vol. 226, no. 2, pp. 378-384

Keywords 

alpha 1 antitrypsinhumannonhumanprotein aggregationprotein foldingalpha 1-Antitrypsinhumans

Abstract 

The folding-unfolding kinetics of human α1-antitrypsin ((α1-AT) were examined by monitoring intrinsic Trp fluorescence and extrinsic ANS fluorescence. While the unfolding of α1-AT followed a single exponential phase, refolding exhibited three exponential phases. The fast phase (T(1,r),< 40 sec), which was independent of urea concentration, appears to be hydrophobic collapse that may be limited by cis-trans isomerization of prolyl residue. The medium phase (T(2,r) = 200 sec) yielded an intermediate (I(N)),which is capable of elastase binding. The slowest (T(3,r), = 1000 sec) phase completes refolding to the native protein, which intersects with the unfolding kinetics at the same urea concentration (1.9 M) as the equilibrium midpoint Concentration-dependence of the amplitude of major refolding phases indicated that IN is prone to kinetic competition between the on-pathway to native protein and aggregation.

ISSN 

0006-291X

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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