Talk:Disulfide bond

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Cytoplasmic disulfide bonds in eukaryotes

The Hatahet et al. paper says that disulfide bonds are not stable in the cytoplasm of E. coli because it is a reducing environment. However, neither that paper nor Sevier et al. say the same about eukaryotes. Certainly the proteins are stable in the endoplasmic reticulum where they are created. There are probably other organelles where they are stable as well. If "usually proteins secreted to the extracellular medium" is true for eukaryotes, an additional source is needed to support this. 140.233.203.193 (talk) 18:17, 2 March 2012 (UTC)[reply]

Cys-cys bonds

Quoting from the text:

When two cysteine amino acids bond to each other, they do so through a disulfide bond.

Ouch. No cys-cys dipeptides? David M

Disulphide bonds in bacteria

I think that the section on disuplhide bonds in bacteria should be made clearer. I am a microbiologist and I'm really unsure to what you are refering when you say as a reversible switch that turns a protein on or off when bacterial cells are exposed to oxidation reactions.

Also bacteria do have the ability to form disulphide bonds but only in the periplasm where it is an oxidizing enviroment.

Nick

Formation rates

Is there any info on rates of formation? Or even some references. This is a complicated question, however it may be good to address it rather than ignore it. For instance: rate of thiol to thiol disulfide formation vs rate of CYS to CYS disulfide formation, etc.

Spamming Wikipedia

Biologicalworld.com has spammed wikipedia like no tomorrow. He is a site of only a few pages and a LOT of adsense. Not much information is given except for "protocols" which are not referenced, and cannot be trusted from a site of that quality.

check: Links from Wikipedia

The following have been cleaned up:

wiki.riteme.site/wiki/Plasmid
wiki.riteme.site/wiki/Gel_electrophoresis
wiki.riteme.site/wiki/Green_fluorescent_protein
wiki.riteme.site/wiki/Homology_(biology)
wiki.riteme.site/wiki/HeLa
wiki.riteme.site/wiki/Protease
wiki.riteme.site/wiki/Restriction_enzyme
wiki.riteme.site/wiki/Petri_dish
wiki.riteme.site/wiki/Structural_domain
wiki.riteme.site/wiki/Trypsin
wiki.riteme.site/wiki/Oligonucleotide
wiki.riteme.site/wiki/Transmission_electron_microscope
wiki.riteme.site/wiki/Agar_plate
wiki.riteme.site/wiki/Calcium_phosphate
wiki.riteme.site/wiki/Disulfide_bond
wiki.riteme.site/wiki/Denaturation_(biochemistry)
wiki.riteme.site/wiki/DNA_ligase
wiki.riteme.site/wiki/Wild_type
wiki.riteme.site/wiki/Tissue_culture
wiki.riteme.site/wiki/Transmission_electron_microscopy
wiki.riteme.site/wiki/Reporter_gene
wiki.riteme.site/wiki/Northern_blot
wiki.riteme.site/wiki/Protein_engineering
wiki.riteme.site/wiki/Sticky_end/blunt_end
wiki.riteme.site/wiki/Taq_polymerase
wiki.riteme.site/wiki/Protein_domain
wiki.riteme.site/wiki/Coomassie
wiki.riteme.site/wiki/Native_state
wiki.riteme.site/wiki/Chinese_Hamster_Ovary_cell
wiki.riteme.site/wiki/Peptidase
wiki.riteme.site/wiki/Visking_tubing
wiki.riteme.site/wiki/Streptavidin
wiki.riteme.site/wiki/Microtiter_plate
wiki.riteme.site/wiki/Subcloning
wiki.riteme.site/wiki/Ion_exchange_chromatography
wiki.riteme.site/wiki/Thermal_cycler
wiki.riteme.site/wiki/Bovine_serum_albumin
wiki.riteme.site/wiki/Phosphate_buffered_saline
wiki.riteme.site/wiki/Glutathione_S-transferase
wiki.riteme.site/wiki/HEPES
wiki.riteme.site/wiki/Ortholog
wiki.riteme.site/wiki/Proteases
wiki.riteme.site/wiki/Salting_out
wiki.riteme.site/wiki/Fetal_bovine_serum
wiki.riteme.site/wiki/Proteolytic_enzyme
wiki.riteme.site/wiki/DNA_end
wiki.riteme.site/wiki/Supernatant
wiki.riteme.site/wiki/ABTS
wiki.riteme.site/wiki/Conserved_sequence
wiki.riteme.site/wiki/Peptide_mass_fingerprinting
wiki.riteme.site/wiki/Dithiothreitol
wiki.riteme.site/wiki/Uranyl_acetate

and many more Sciencetalks (talk) —Preceding comment was added at 03:03, 4 January 2008 (UTC)[reply]

Corrections needed

There are quite a few mistakes in this article. I have fixed some, but many remain. For example, it can't be stated that in-vivo disulfide rearrangement reactions (or other reactions involving disulfides) are intra-molecular. Disulfide formation/destruction/isomerization is generally a catalyzed process in living cells, and catalysis usually involves formation of inter-molecular mixed disulfide bond with the catalyst. I hope to find some time to add a section on how disulfide bonds are formed and destroyed in different compartments of prokaryotic and eukaryotic cells. The importance of disulfide bonds in living organisms is understated. For example, the production of deoxyribonucleotides (building blocks of the genetic code) involves an enzyme called ribonucleotide reductase, with a disulfide bond at it's catalytic heart. The numbering of the figures should be removed, as now some figures are numbered while others are not. Thioredoxins usually do not have vicinal Cys. The catalytic motif in Trx is CXXC. It usually participates in the reduction of disulfide bonds in cytoplasm with an indirect role of oxidation of extracytoplasmic proteins through an electron relay such as DsbD in E. coli. Naming cytoplasm (redox potential ~-300 mV) as reducing environment and e.g. endoplasmic reticulum (-160 mV) as oxidizing is misleading, i.e. standard redox potential of oxygen (O2) is +620 mV.

Fermmyt (talk) 23:35, 4 October 2013 (UTC)[reply]