Native disulfide bond formation in proteins

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Native disulfide bond formation in proteins.

Native disulfide bond formation is critical for the proper folding of many proteins. Recent studies using newly identified protein oxidants, folding catalysts, and mutant cells provide insight into the mechanism of oxidative protein folding in vivo. This insight promises new strategies for more efficient protein production.

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Small-molecule Catalysis of Native Disulfide Bond Formation in Proteins

Native disulfide bond formation is essential for the folding of many proteins. The enzyme protein disulfide isomerase (POI) catalyzes native disulfide bond formation using a Cys-Gly-HisCys active site. The active-site properties of POI (thiol pK. = 6.7 and disulfide E;O' = -180 mY) are critical for efficient catalysis. This Dissertation describes the design, synthesis, and characterization of s...

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Cellular Disulfide Bond Formation in Bioactive Peptides and Proteins

Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics. These peptides often possess disulfide bonds, which are important for their structure, function and stability. A systematic network of enzymes--a disulfide bond generating enzyme, a disulfide bond donor enzyme and a redox cofactor--that function inside the cell dictates the formatio...

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Disulfide bond formation in the eye lens.

The disposition and disposal of the -SH groups of the lens during aging and cataractogenesis have been investigated by laser Raman spectroscopy as a noninvasive microprobe in the intact living lens. In this procedure -SH and -S-S- give unique discrete Raman signals (at 2580 and 508 cm-1) that may be used to calculate relative concentrations in a very small volume of the lens. We present evidenc...

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Rapid formation of the native 14-38 disulfide bond in the early stages of BPTI folding.

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ژورنال

عنوان ژورنال: Current Opinion in Chemical Biology

سال: 2000

ISSN: 1367-5931

DOI: 10.1016/s1367-5931(00)00128-9