Talk:Denaturation (biochemistry)

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Wiki Education Foundation-supported course assignment

This article was the subject of a Wiki Education Foundation-supported course assignment, between 28 January 2019 and 13 May 2019. Further details are available on the course page. Student editor(s): Kevyeung55.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 19:57, 17 January 2022 (UTC)[reply]

Wiki Education Foundation-supported course assignment

This article is or was the subject of a Wiki Education Foundation-supported course assignment. Further details are available on the course page. Student editor(s): Stephanietepan18, SarhAly 378. Peer reviewers: Stephanietepan18, SarhAly 378.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 19:18, 16 January 2022 (UTC)[reply]

From Talk:Denatured

Is gelatin denatured collagen? Both have very high glycine content. -phma

since it is capable of a gel to sol transition, I would have to say no. This is a blurb about gelatin from http://www.gelatine.org :

Gelatine is a pure protein obtained from animal raw materials containing collagen. The natural and healthy food has excellent gelling strength.

Dwmyers 16:16 Feb 12, 2003 (UTC)

Another example that could be added, if it isn't too grisly: if my information is correct, denaturation is why you wash blood stains in cold water. Using hot water on blood denatures it, causing protein strands to twist around fibers in the fabric, making them almost impossible to remove. Using cold water to clean blood out of cloth works pretty well.

I heard that you can prepare fish like tuna and salmon by marinating them in lemon juice over night as opposed to cooking with heat. Anyone know more information about this? I assume it's an example of denaturation.

same as the ceviche example

H-bonding in secondary structure

I believe that it should be noted that the disruption of secondary structure is due to the breaking of hydrogen bonds between the amino acid residues. This is important because it is the localized hydrogen bonding that lets amino acids form the secondary structures that they do. —Preceding unsigned comment added by 130.126.68.140 (talk) 22:02, 18 September 2007 (UTC)[reply]

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

Please help me with this someone or get a bot to delete the spam.

The following have been cleaned up:

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

and many more Sciencetalks (talk) —Preceding comment was added at 03:05, 4 January 2008 (UTC)[reply]

If you find a URL that is added as spam to articles you can take it to m:Talk:Spam blacklist. ----Seans Potato Business 12:58, 28 January 2008 (UTC)[reply]

Denatured proteins in eggs

So if the protein in eggs is denatured by cooking it, does this mean that a cooked egg's protein is still valuable to the body (even if not as valuable as a raw egg)? And do different cooking methods (i.e microwaving) make the protein in eggs even less nutritious? Kitty (talk) 09:07, 15 September 2009 (UTC)[reply]

Denaturation does not alter the primary structure of the protein (the amino acid sequence). The protein that you eat is digested to yield individual amino acids that are used by your body to synthesise its own proteins (OSB 2011)

Denaturing Eggs

Page says "Although denaturing egg whites is irreversible, in many other cases denaturing is reversible", but I don't think that's true. Molecular Gastronomy has figured out you can unboil an egg, which if my understanding is correct, means that you've reversed the denaturing process. Sodium borohydride is the preferred chemical for the process, but Vitamin C can work, too. Hardburn (talk) 14:04, 24 November 2009 (UTC)[reply]

Another article discussing the process of unboiling an egg / renaturing the proteins in the white. Harp2812 (talk) 20:08, 26 January 2015 (UTC)[reply]

Common Examples

"Pouring egg whites into a beaker of acetone will also turn egg whites translucent and solid." Shouldn't this read "opaque and solid"? Zalumon (talk) 18:37, 21 September 2012 (UTC)[reply]

Proposed merge with Coagulated protein

A mere dictionary definition for a minor concept in protein denaturation. הסרפד (call me Hasirpad) 18:35, 9 June 2015 (UTC)[reply]

Assessment comment

The comment(s) below were originally left at Talk:Denaturation (biochemistry)/Comments, and are posted here for posterity. Following several discussions in past years, these subpages are now deprecated. The comments may be irrelevant or outdated; if so, please feel free to remove this section.

I find the word "denaturating" commonly used, but it would appear to be incorrect... Would any biochemistry experts out there like to comment on a possible distinction between denaturing and denaturating? Is this error as widespread as it seems, or is a "denaturating buffer" different in some way from a "denaturing buffer?"

Last edited at 09:44, 6 August 2007 (UTC). Substituted at 13:11, 29 April 2016 (UTC)

Suggested Edits (Content, Sources)

In the introduction of this article there is mention to several conditions that can cause denaturation. The ones listed were as follows: external stress from an acid or base, inorganic salts, organic solvents, radiation and heat. The common denaturation section mentions just the egg example. I agree that this is a great tangible and visible example of denaturation. I do think that possible adding more examples in this section may be beneficial. The examples could possibly expand on one of the other factors listed that can cause denaturation.

When searching through the citations, I noticed that one of the sources, source 5, was from 1968. After reading the article it seems that it may be outdated. The article mentions doubt had by the researchers that seems to be more supported by studies today. For example, the article seems to only confirm that denaturation indeed removes secondary, tertiary, and quaternary structure. A more recent article may be able to expand on this discovery possibly allowing answers to the how and why aspects of this discovery.

(Belles18 (talk) 04:19, 3 September 2016 (UTC))[reply]

"Currently" (as of 2003)

In § Biologically-induced denaturation, the text currently says

Currently, biophysical and biochemical research studies are being performed to more fully elucidate the thermodynamic details of the denaturation bubble[,]

and cites

Altan-Bonnet, Grégoire; Libchaber, Albert; Krichevsky, Oleg (1 April 2003). "Bubble Dynamics in Double-Stranded DNA". Physical Review Letters. 90 (13). doi:10.1103/physrevlett.90.138101.

While I have little doubt that this is true, "currently" is an inherently time-sensitive word—so a nearly 15-year-old reference doesn't seem like the ideal choice! There's probably a better, less time-sensitive, way to word the sentiment, but I'm not sure what. Any ideas? dendodge 10:53, 14 December 2017 (UTC)[reply]

Protein Denaturation - Acid and Bases

Hello all, I hope all is well. I had a suggestion for this article. I noticed that their was no section on how acids and bases can denature proteins. I was wondering if I could be please help edit this article to include this section. Please let me know what you think. Thank you once again.Stephanietepan18 (talk) 23:42, 30 April 2018 (UTC)[reply]

Protein Denaturation

Hello editors, it came to my notice that there was not a section on techniques of protein denaturation. I was hoping to know if it would be acceptable that I incorporate some of these techniques to the article. Please let me know what you think. SarhAly 378 (talk) 23:42, 30 April 2018 (UTC)[reply]

Wiki Education assignment: CHEM 378 - Biochemistry Lab

This article was the subject of a Wiki Education Foundation-supported course assignment, between 25 August 2022 and 15 December 2022. Further details are available on the course page. Student editor(s): Apple F1 (article contribs).

— Assignment last updated by Apple F1 (talk) 23:23, 7 December 2022 (UTC)[reply]