The growth hormone receptor contains seven cysteine residues in its extracellular domain. The six in the growth hormone binding domain form disulfide bonds, and help the receptor to gain its correct three-dimensional structure. In this study we replaced the cysteine for serine and alanine residues and investigated their role in growth hormone receptor folding, dimerisation and signal transducti...

Using recombinant variants of BPTI, we have determined the rate constants corresponding to formation of each of the fifteen possible disulfide bonds in BPTI, starting from the reduced, unfolded protein. The 14-38 disulfide forms faster than any of the other 14 possible disulfides. This faster rate results from significantly higher intrinsic chemical reactivities of Cys-14 and Cys-38, in additio...

A molecule of rabbit yG-globulin’ evidently consists of four polypeptide chains held together by interchain disulfide bonds and noncovalent interactions. Each molecule comprises a pair of similar or identical “light” chains having an approximate molecular weight of 20,000, and another pair of “heavy” chains of weight 50,000 to 55,000 (2-7). Each light chain is linked to a heavy chain and the tw...

The membrane-anchored thioredoxin-like protein (TlpA) from the Gram-negative soil bacterium Bradyrhizobium japonicum was initially discovered due to its essential role in the maturation of cytochrome aa3. A soluble form of TlpA lacking the N-terminal membrane anchor acts as a protein thiol:disulfide oxidoreductase. TlpA possesses an active-site disulfide bond common to all members of the thiol:...

Mutant human lysozymes (HLZ) lacking two disulfide bonds were constructed to study the importance of each disulfide bond on oxidative refolding. To avoid destabilization, a calcium-binding site was introduced. Five of the six species of two-disulfide mutants could be obtained with enzymatic activity. Based on the information obtained from refolding and unfolding experiments, the order of import...

8 3.1. Catalysis of oxidative protein folding 8 3.2 De novo formation of disulfide bonds in E. coli: the discovery of DsbA 9 3.3. DsbA is the most oxidizing disulfide catalyst 11 3.4. DsbB provides the periplasm with oxidizing power 15 3.5. Correcting wrong disulfide bonds in the periplasm: disulfide bond isomerization by DsbC 18 3.6. DsbD provides reducing equivalents in a highly oxidizing env...

A molecule of rabbit yG-globulin’ evidently consists of four polypeptide chains held together by interchain disulfide bonds and noncovalent interactions. Each molecule comprises a pair of similar or identical “light” chains having an approximate molecular weight of 20,000, and another pair of “heavy” chains of weight 50,000 to 55,000 (2-7). Each light chain is linked to a heavy chain and the tw...

Glial cell line-derived neurotrophic factor (GDNF) is a member of the TGF-beta superfamily of proteins. It exists as a covalent dimer in solution, with the 15 kDa monomers linked by an interchain disulfide bond through the Cys101 residues. Sedimentation equilibrium and velocity experiments demonstrated that, after removal of the interchain disulfide bond, GDNF remains as a non-covalent dimer an...