Production of disulfide-linked hirudin dimer by in vitro folding
نویسندگان
چکیده
منابع مشابه
The disulfide folding pathway of hirudin elucidated by stop/go folding experiments.
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...
متن کاملDisulfide-linked protein folding pathways.
Determining the mechanism by which proteins attain their native structure is an important but difficult problem in basic biology. The study of protein folding is difficult because it involves the identification and characterization of folding intermediates that are only very transiently present. Disulfide bond formation is thermodynamically linked to protein folding. The availability of thiol t...
متن کاملElucidation of the disulfide-folding pathway of hirudin by a topology-based approach.
A theoretical model for the folding of proteins containing disulfide bonds is introduced. The model exploits the knowledge of the native state to favor the progressive establishment of native interactions. At variance with traditional approaches based on native topology, not all native bonds are treated in the same way; in particular, a suitable energy term is introduced to account for the spec...
متن کاملProduction of Iron Disulfide Nanoparticles by Hydrothermal Process
In this research, a single-stage low-temperature hydrothermal synthesis route was successfully developed for preparation of Iron Disulfide. The prepared powder was characterized by X-ray diffraction (XRD) and scanning electron microscopy (SEM). These analyses showed that nanoparticles were well crystallized, pyrite was the main product and the shape of crystals was nanorod. Also, the influences...
متن کاملOxidative 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 ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1993
ISSN: 0014-5793
DOI: 10.1016/0014-5793(93)81607-2