Oxidative folding of hirudin in human serum

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Oxidative folding of hirudin in human serum.

Human serum contains factors that promote oxidative folding of disulphide proteins. We demonstrate this here using hirudin as a model. Hirudin is a leech-derived thrombin-specific inhibitor containing 65 amino acids and three disulphide bonds. Oxidative folding of hirudin in human serum is shown to involve an initial phase of rapid disulphide formation (oxidation) to form the scrambled isomers ...

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Controlling the speed of hirudin folding.

The folding of hirudin undergoes an initial stage of non-specific packing, followed by consolidation (re-organization) of partially packed intermediates to attain the native structure [Chatrenet and Chang (1993) J. Biol. Chem. 268, 20988-20996]. Non-specific packing leads to the formation of scrambled hirudins as folding intermediates. A systematic study was carried out to search for conditions...

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The folding pathway of hirudin was analyzed by structural characterization and stop/go folding experiments of acid-trapped intermediates. The results show that the folding is initiated by a near-random packing, followed by the reorganization and fine adjustment of partially compact intermediates to attain the active molecule. The process of packing is observed as the unfolded hirudin flows sequ...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2006

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj20051660