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Protein disulfide bonding

Freedman, R.B. The formation of protein disulfide bonds. Curr. Opin. Struct. Biol. 5 85-91, 1995. [Pg.119]

Witkiewicz, P.L. and Shaw, C.F. Ill (1981) Oxidative cleavage of peptide and protein disulfide bonds by gold(III) amechanism for gold toxicity. Journal of the Chemical Society, Chemical Communications, (21), 1111-1114. [Pg.317]

Gorman J.J., Wallis T.P., and Pitt J.J. (2002), Protein disulfide bond determination by mass spectrometry, Mass Spectrom. Rev. 21, 183-216. [Pg.276]

Inhibits serine proteases such as trypsin and chymotrypsin. Also inhibits cysteine proteases (reversible by reduced thiols) and mammalian acetylcholinesterase Inhibits ATPase, alkaline phosphatase and tyrosine phosphatase Reagent for maintaining -SH groups in the reduced state. Effective for reducing protein disulfide bonds prior to SDS-PAGE... [Pg.204]

Anfinsen, C. B., and E. Haber Studies on the reduction and re-formation of protein disulfide bonds. Journ. Biol. Chem. 236, 1361—1.363 (1961). [Pg.34]

Cline DJ, et al. New water-soluble phosphines as reductants of peptide and protein disulfide bonds reactivity and membrane permeability. Biochemistry 2004 43 15195. [Pg.125]

Analogous to the electrode behavior of cystine and cysteine, one may expect chemical reaction occurring between mercury and protein disulfide bonds. Honeychurch and Ridd [99] have proved the correctness of such reaction pathway, applying poten-tiometric stripping analysis to investigate... [Pg.974]

The acetate/saline buffer was originally used for the column chromatography of the derivatized RIP because the S-pyridyl group is easily displaced by sulfhydryl reagents under the conditions of low pH at which protein disulfide bonds are relatively stable. Most single-chain RIPs are stable to these conditions. [Pg.140]

The major type of PTM that has this function is protein disulfide bond formation (33). Disulfide bonds are more stable thermodynamically than the reduced thiols in an oxidizing environment. In eukaryotes, proteins that undergo the secretary pathway start to form disulfide bonds once they are translocated into the endoplasmic recticulum (ER) lumen, which is an oxidizing environment. These disulfide bonds help to stabilize... [Pg.1558]

Kadokura H, Katzen E, Beckwith J. Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 2003 72 111-135. 59. [Pg.1577]

El Hanine, Lmoumene C., Conte D., Jacquot J.-R, Houee-Levin C., Redox properties of protein disulfide bond in oxidized thioredoxin and lysozyme. A pulse radiolysis study. Biochemistry, 2000,39,9295-9301. [Pg.246]

Prinz, W. A., Aslund, F., Holmgren, A., and Beckwith, J. (1997). The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm./. Biol. Chem. 272, 15661-15667. [Pg.387]

The efficient formation of disulfide bonds In the lumen of the ER depends on the enzyme protein disulfide isomerase (PDI), which Is present In all eukaryotic cells. This enzyme Is especially abundant In the ER of secretory cells In such organs as the liver and pancreas, where large quantities of proteins that contain disulfide bonds are produced. As shown in Figure 16-19a, the disulfide bond in the active site of PDI can be readily transferred to a protein by two sequential thiol-disulfide transfer reactions. The reduced PDI generated by this reaction is returned to an oxidized form by the action of an ER-resident protein, called Erol, which carries a disulfide bond that can be transferred to PDI. It is not yet understood how Erol itself becomes oxidized. Figure 16-20 depicts the organization of the pathway for protein disulfide-bond formation In the ER lumen and the analogous pathway In bacteria. [Pg.675]

The enzyme, found in a number of plant tissues, reduces the disulfide bonds in a number of proteins. Its activity is strongly inhibited by sulfhydryl reagents. The enzyme is different from cystine reductase and glutathione reductase which do not reduce protein disulfide bonds. [Pg.112]

The disulfide formation depends on the protein conformation that places Cys residues into appropriate proximity and the disulfide redox potential that determines the intrinsic stability of protein disulfide bonds. For catalytic activity, the reduced dithiol form of protein disulfide isomerase is required. Protein disulfide isomerase is a folding catalyst that assists protein folding (Gilbert, 1997). The enzyme increases the rate of the overall folding process of the substrate protein without altering its pathway. [Pg.487]

The ER is endowed with chaperones, protein disulfide isomerases and glycosylation enzymes, as well as their accessory proteins. Disulfide bond formation has frequently been observed to constitute a major bottleneck, and the overexpression of PDIl alone or in combination with its oxidase EROl was shown to enhance productivity of several proteins in P. pastoris [95, 119-123]. Also, the reinforcement of other ER-related processes was assessed with variable success [124, 125]. In particular, overproduction of Kar2 yielded unpredictable results, which can be explained by its cellular function as a signal molecule of the UPR... [Pg.701]

Ganisl, B., Breuker, K. (2012) Does electron capture dissociation cleave protein disulfide bonds ... [Pg.164]

In proteins, cysteines form disulfide bond and exist as cystine units (dimer of cysteine) which is one of the causes of helicity of proteins. Keeping in mind the strong affinity of Au towards sulfur, it is assumed that Au ions bind to cysteine residues of the proteins. When Au ions are uptaken by the protein, disulfide bonds break and protein secondary structure is lost. This process can help the bare clusters to achieve their stability in gas phase. This was explained taking Auss as a model through density functional theory calculations. [Pg.377]

Figure 9. Mechanism for base-catalyzed transformation of a protein disulfide bond to two dehydroalanine side chains, a sulfide ion, and sul r. Figure 9. Mechanism for base-catalyzed transformation of a protein disulfide bond to two dehydroalanine side chains, a sulfide ion, and sul r.
Figure 10. Mechanism for base-catalyzed formation of one dehydroalanine residue, and one persulfide ion from a protein disulfide bond. The persulfide can decompose to a thiolate anion and elemental sulfur. Figure 10. Mechanism for base-catalyzed formation of one dehydroalanine residue, and one persulfide ion from a protein disulfide bond. The persulfide can decompose to a thiolate anion and elemental sulfur.
The tertiary structure of the proteins is the 3D organisation of the proteins, involving the repartition of the secondary structure units of the proteins with respect to each other. The driving force for the folding into tertiary structure is dependent on the physicochemical properties of the medium. In aqueous solutions, the hydro-phobic residues of the proteins are hidden in the core of the proteins in order to minimise contacts with water molecules. The protein tertiary structure is stabilised by hydrophobic interactions, salt bridges, hydrogen bonds and, for some proteins, disulfide bonds. [Pg.72]


See other pages where Protein disulfide bonding is mentioned: [Pg.184]    [Pg.136]    [Pg.1047]    [Pg.397]    [Pg.313]    [Pg.46]    [Pg.150]    [Pg.129]    [Pg.5451]    [Pg.249]    [Pg.182]    [Pg.93]    [Pg.351]    [Pg.95]    [Pg.88]    [Pg.447]    [Pg.5450]    [Pg.143]    [Pg.76]    [Pg.77]    [Pg.301]    [Pg.46]    [Pg.266]    [Pg.76]    [Pg.664]   
See also in sourсe #XX -- [ Pg.109 ]




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Bonded proteins

Bonds disulfides

Disulfide bonds

Disulfide bonds in proteins

Disulfide bonds proteins lacking

Disulfide bonds unfolded protein state

Disulfide bonds, protein folding mechanism

Disulfide bonds, proteins with

Disulfide proteins

Disulfide-bonded proteins, synthesis

Prion protein disulfide bond

Protein bonds

Protein bonds disulfide

Protein bonds disulfide

Protein digestibility disulfide bonding

Protein disulfide bond reduction

Protein disulfides

Protein sequencing disulfide bond cleavage

Protein sequencing disulfide bond position

Protein structures, disulfide bonding

Proteins bonding

Proteins disulfide bond cleavage

Proteins stability disulfide bond

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