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Disulfide Bond Formation in the Cytoplasm
Antioxidants & Redox Signaling, 2013Disulfide bond formation is critical for biogenesis of many proteins. While most studies in this field are aimed at elucidating the mechanisms in the endoplasmic reticulum, intermembrane space of mitochondria, and prokaryotic periplasm, structural disulfide bond formation also occurs in other compartments including the cytoplasm.
Mirva J, Saaranen, Lloyd W, Ruddock
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Nondissociative Electron Capture by Disulfide Bonds
The Journal of Physical Chemistry A, 2001By means of Rydberg electron-transfer spectroscopy (RETS), negative ion photoelectron spectroscopy (NIPES), and quantum chemistry calculations, we have studied electron attachment properties of a s...
Carles, S. +8 more
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Disulfide Bond Mimetics: Strategies and Challenges
Chemistry – A European Journal, 2017AbstractThe activity profile of many biologically relevant proteins and peptides often relies on a precise 3D structural organization. In this context, disulfide bonds are natural covalent constraints that play a key role in driving and stabilizing the folding pattern of these molecules.
Gori A, Gagni P, Rinaldi S
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THE GENETICS OF DISULFIDE BOND METABOLISM
Annual Review of Genetics, 1998▪ Abstract Disulfide bonds are required for the stability and function of a large number of proteins. Genetic analysis in combination with biochemical studies have elucidated the main catalysts involved in facilitating these processes in the cell. All enzymes involved in thiol-disulfide metabolism have a conserved active site that consists of two ...
A, Rietsch, J, Beckwith
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Engineering disulfide bonds within an antibody
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2014Antibodies have evolved to function in oxidative, extracellular environments. A pair of cysteines in close proximity will oxidatively react to form a disulfide bond that fixes and stabilizes the tertiary structure of a protein. Immunoglobulin G (IgG) includes several disulfide bonds, and the patterns of inter-chain disulfide bonds characterize ...
Yoshihisa, Hagihara, Dirk, Saerens
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Cooperative disulfide bond formation in apamin
Biochemistry, 1992Apamin is being studied as a model for the folding mechanism of proteins whose structures are stabilized by disulfide bonds. Apamin consists of 18 amino acid residues and forms a stable structure consisting of a C-terminal alpha-helix and two reverse turns.
M H, Chau, J W, Nelson
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Disulfide bond formation in proteins
1984Publisher Summary Protein disulfide formation in vivo as a post-translational modification is expected to depend upon both the conformation and the environment of the polypeptide chain during and after biosynthesis. Extrapolations from in vitro results may be informative, but the in vivo process should be amenable directly to study with the ...
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Cytoglobin conformations and disulfide bond formation
The FEBS Journal, 2010The oligomeric state and kinetics of ligand binding were measured for wild‐type cytoglobin. Cytoglobin has the classical globin fold, with an extension at each extremity of about 20 residues. The extended length of cytoglobin leads to an ambiguous interpretation of its oligomeric state. Although the hydrodynamic diameter corresponds to that of a dimer,
Lechauve, Christophe +7 more
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Disulfide Bond Formation Enzymes
2007Publisher Summary This chapter discusses the disulfide bond (Dsb) formation and isomerization in the periplasm of the model organism E.coli and focuses on the enzymatic properties of disulfide catalysts and isomerases. Disulfide bond formation and isomerization are catalyzed processes in both prokaryotes and eukaryotic organisms, and the enzymes ...
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Methods to monitor mitochondrial disulfide bonds
Mitochondria contain numerous proteins that utilize the chemistry of cysteine residues, which can be reversibly oxidized. These proteins are involved in mitochondrial biogenesis, protection against oxidative stress, metabolism, energy transduction to adenosine triphosphate, signaling and cell death among other functions.Ben Hur Marins, Mussulini +2 more
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