Search for dissertations about: "disulfide bond formation"

Showing result 1 - 5 of 18 swedish dissertations containing the words disulfide bond formation.

2. 1. Membrane-bound thiol-disulfide oxidoreductases in Bacillus subtilis

   Author : Lydur Erlendsson; Institutionen för experimentell medicinsk vetenskap; []
   Keywords : MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; virologi; mykologi; Mikrobiologi; mycology; virology; bacteriology; Microbiology; sporulation; cytochrome c; thiol-disulfide oxidoreductases; Bacillus subtilis; membrane proteins; bakteriologi;

   Abstract : Disulfide bonds in proteins are found between cysteine residues and are usually important for either function or stability of proteins. Thiol-disulfide oxidoreductases catalyse the formation or breakage of disulfide bonds in proteins. READ MORE

4. 2. Studies on Thiol-Disulfide Oxidoreductases in Bacillus subtilis

   Author : Mirja Carlsson Möller; Molekylär cellbiologi; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES; virology; mycology; Mikrobiologi; bakteriologi; virologi; mykologi; Microbiology; bacteriology; bacterial sporulation; endospore; thioredoxin; Thiol-disulfide oxidoreductase;

   Abstract : Bacillus subtilis is a model organism for endospore-forming gram-positive bacteria. Endospores are formed in response to nutrient starvation. They can resist harsh environments and last for long periods of time. Once nutrients again become available, the endospore can germinate and the vegetative life cycle be resumed. READ MORE

5. 3. Protein disulfide isomerase : function and mechanism in oxidative protein folding

   Author : Ruoyu Xiao; Karolinska Institutet; Karolinska Institutet; []
   Keywords : Protein disulfide isomerase; endoplasmic reticulum; protein folding;

   Abstract : The formation of native intramolecular disulfide bonds is critical for the folding and stability of many secreted proteins. This process involves oxidation of protein thiols to form disulfide bonds as well as rearrangement of any non-native disulfide bonds that might form. READ MORE

6. 4. Production and folding of proteins in the periplasm of Escherichia coli

   Author : Rageia Elfageih; Jan-Willem de Gier; Hans-Georg Koch; Stockholms universitet; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES; Escherichia coli; periplasm; recombinant protein production; disulfide bond containing proteins; translation initiation region; protein translocation machinery; co-translational folding; neuraminidases; biokemi; Biochemistry;

   Abstract : The Gram-negative bacterium E. coli is the most widely used host for the production of recombinant proteins. Disulfide bond containing recombinant proteins are usually produced in the periplasm of E. coli since in this compartment of the cell - in contrast to the cytoplasm - disulfide bond formation is promoted. READ MORE

7. 5. Identification of the domains of disulfide interaction in the mammalian ribosomal proteins L6 and L29

   Author : Heinz Nika; Stockholms universitet; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES;

   Abstract : The 60-S subunits of mammalian ribosomes contain two adjacent proteins, identified as L6 and L29, which interact reversibly in situ by disulfide bond formation. The disulfide complex and the individual proteins were prepared by polyacrylamide gel electrophoresis under non-oxidizing conditions for effective prevention of methionine oxidation. READ MORE