Talk:Protein folding

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Is there a way to simplify the explanation of the process? The 'middle-school English' explanation (which of course, has since been deleted)was actually a good summary without having to go deep into the complexity.

I'm not sure my biochemistry is up to it, but should something about the different levels of protein structure be added here, (primary, secondary, tertitary etc.)?

The main protein article has that - I suppose you could refer to that article. -- Marj 05:44, 26 Oct 2003 (UTC) ok

I've tried to make the initial section a bit clearer but it's a difficult thing to provide a non-technical summary of. I've also put in some references to (mostly) free articles & books. Hopefully it doesn't jump in quite so quickly now. See what you think. MockAE 12:34, 14 April 2007 (UTC)

Contents 1 Folding temperature 2 H-bonds, entropy, etc. 3 Techniques for studying protein folding 4 Random coil --> Random coil (protein folding)

[edit] Folding temperature

I have read that the folding temperature of a protein is defined as the temperature at which there is a peak in the heat capacity of the protein. I am not sure what this means physically about what is different in the protein at the folding temperature versus below the folding temperature. However, I would like very much to know. Thank you. —Preceding unsigned comment added by Shindizzle (talk • contribs)

This page is useless. If anyone could understand this page, they wouldn't need Wikipedia to explain it to them. —Preceding unsigned comment added by 76.215.213.229 (talk)

The folding temperature is a minor point in the grand scheme of protein folding. FYI, it is a characteristic temperature at which the protein spends half the time in the folded state and half the time in the unfolded state. The peak of the heat capacity for any substance (protein or otherwise) is the temperature at which the transition from one state to another occurs (e.g. phase transition). So, for proteins, the peak is the temperature at which the protein goes from the unfolded state to the folded state. —Preceding unsigned comment added by 66.122.236.163 (talk)

That's not entirely correct. The temperature at which the protein spends half the time in the folded state and half the time in the unfolded state is the ' folding transition temperature for a two state folding protein '. The term 'folding temperature' is an imprecise term. --159.178.50.165 (talk) 15:41, 10 March 2008 (UTC)

external link to rosetta is needless- they do not study the protein folding. they predict final structure, ant this should be addressed to "protein structure prediction" . this also refers to human proteom folding project, predictor at home, fight aids at home and all others. only Stanford is studying the protein folding. 84.15.64.164 12:30, 8 May 2006 (UTC)Samurajus712

[edit] H-bonds, entropy, etc.

This is a nice article, although it could be done more "in depth". H-bonds do stabilize protein structure. The catch: water is liquid. When water freezes itself, there is a certain energy gain called enthalpy of fusion. This enthalpy of fusion originates mostly from formation of H-bonds between molecules of water: these H-bonds are strong in the solid state, but "transient" in the liquid mobile water. Same thing with protein folding, helix-coil transitions, crystallization, etc. The energy of H-bond in protein folding is ~-1.5 kcal/mol (mutagenesis and other data). Main force that opposes protein folding is conformational entropy (like in any other liquid to solid state type transition). This is easy to fix. I can do this later. Biophys 17:26, 28 October 2006 (UTC)

[edit] Techniques for studying protein folding

It would be good to separate experimental and computational techniques. There are many more experimental methods that should be mentioned here. Biophys 18:03, 29 October 2006 (UTC)

It is important to tell something about protein folding pathways based on experimental data (intermediates, transition states, etc.), about thermodynamic stability of proteins, and differences between water-soluble and transmembrane proteins. Beta-sheet is not a secondary structure! The beta-strand is. Biophys 04:08, 2 November 2006 (UTC)

Disulfide bonds often exist within beta sheets, and sometimes even within alpha helices. This is corrected. Biophys 02:07, 4 November 2006 (UTC)

[edit] Random coil --> Random coil (protein folding)

Does anyone else think it might be useful to split the random coil article into 2 separate articles? With the first being used to describe the mathematical theory, and the second to describe the protein related aspects of the model?--69.118.143.107 (talk) 18:32, 30 December 2007 (UTC)