Will all proteins fall apart by exaggerated heat?

In summary: I'm not really sure how to say it. Anyway, they are more resistant to external forces than the first two, and denaturation is a process where proteins or nucleic acids lose the tertiary structure and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), or heat.
  • #1
Gliese123
144
0
Like the topic; if you boil proteins (or vitamines for that matter), will the molecular structure break?
For example warm milk etc.
 
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  • #2
With sufficient temperature, all chemical bonds break apart. Even before that happens, proteins can change their shape. I would expect that boiling water at atmospheric pressure is sufficient for most proteins to get modified in some way.
 
  • #3
Gliese123 said:
Like the topic; if you boil proteins (or vitamines for that matter), will the molecular structure break?
For example warm milk etc.

You might be interested in a process called denaturation.


http://en.wikipedia.org/wiki/Denaturation_%28biochemistry%29

Denaturation is a process in which proteins or nucleic acids lose the tertiary structure and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), or heat
 
  • #4
There are many levels of structure in a protein. Your question is not really specific enough.

Heat will denature proteins, meaning there will be enough thermal motion to overcome the H-bonds stabilizing things like helices and sheets and how they are arranged in space etc (referred to as secondary and tertiary structure). There are other interactions of proteins which are more resistant to just heat. For instance when running SDS-PAGE gels, you denature proteins with heat but add some type of reducing agent such as dithiothreitol of mercaptoethanol in order to reduce disulfide bridges which are covalent and fairly stable to heat. Note we are talking reasonable temperatures here, say up to 100 degrees C. Throwing a protein into the sun will yield a different outcome than in a boiling water bath.

Other covalent bonds in proteins are even more stable to physical and chemical perturbations. For instance the peptide bond is so strong that if you want to digest a protein without using peptidases, you boil it for hours and hours in 6M HCl and then hope you have fully digested the protein. There are yet other covalent bonds such as C-C bonds etc, which are pretty much stable to anything you can throw at them short of combustion or some such thing.

So the proteins in milk don't necessarily "fall apart" upon heating or boiling, but they may denature or rearrange to a different configuration from the native one. It really comes down to what you mean when you say fall apart. Perhaps you may be more specific with your question, because "fall apart" can be interpreted in many different ways.
 
  • #5
Thanks a lot for your informative answers. Yes, well we have all heard about "can I boil this without the nutrients breaking up" etc. Sorry for not being especially specific. I suppose I meant boiling in water more exactly.
 
  • #6
Yanick said:
There are many levels of structure in a protein. Your question is not really specific enough.

Heat will denature proteins, meaning there will be enough thermal motion to overcome the H-bonds stabilizing things like helices and sheets and how they are arranged in space etc (referred to as secondary and tertiary structure). There are other interactions of proteins which are more resistant to just heat. For instance when running SDS-PAGE gels, you denature proteins with heat but add some type of reducing agent such as dithiothreitol of mercaptoethanol in order to reduce disulfide bridges which are covalent and fairly stable to heat. Note we are talking reasonable temperatures here, say up to 100 degrees C. Throwing a protein into the sun will yield a different outcome than in a boiling water bath.

Other covalent bonds in proteins are even more stable to physical and chemical perturbations. For instance the peptide bond is so strong that if you want to digest a protein without using peptidases, you boil it for hours and hours in 6M HCl and then hope you have fully digested the protein. There are yet other covalent bonds such as C-C bonds etc, which are pretty much stable to anything you can throw at them short of combustion or some such thing.

So the proteins in milk don't necessarily "fall apart" upon heating or boiling, but they may denature or rearrange to a different configuration from the native one. It really comes down to what you mean when you say fall apart. Perhaps you may be more specific with your question, because "fall apart" can be interpreted in many different ways.
Thanks a lot Yanick. Even though I read about this at school at the moment, I didn't really understand all of what you wrote here but I'll try to understand. :) Thx! Very appreciated
 
  • #7
Sorry if I used language that may be a bit over your head.

Here's the takeaway from what I wrote above. I presented my argument somewhat from a top down approach, here it is from a bottom up approach.

atoms -> molecules/amino acids -> peptides -> proteins -> multi-peptide proteins.

The last three exhibit extra levels of organization such as primary, secondary, tertiary and quaternary structure. Briefly, primary structure of a protein is simply just the sequence of amino acids read in a particular direction. Secondary structure refers to how the "string" will arrange itself into things like helices, turns, loops, sheets etc. Tertiary refers to how the secondary structure elements are arranged in space. Finally quaternary structure refers to how two different (or identical) proteins arrange themselves in space if they happen to interact with one another.

Basically you're question is vague because "falling apart" can mean going from a protein, say hemoglobin (which displays all 4 levels of protein structure), to just atoms of C, H, N, O, S etc.

Something like heat denaturation can go all the way to unwinding the protein where it loses its secondary through quaternary structure but still remains a chain of amino acids. You can go further and start cutting up the "string" into individual amino acids (or shorter strings of amino acids), this takes more than just a bit of boiling as you must break peptide (AKA amide) bonds which are pretty strong bonds. Typically this requires something like an enzyme which cuts peptides up known as a peptidase or very harsh conditions such as boiling in concentrated acid for a long time.

You can also go on to say, I want to break each individual amino acid up into smaller molecules, this takes much more effort because bonds like C-C, C-H etc are extremely strong and stable. You can still do something like breaking a protein down where your products are not amino acids but even smaller molecules by combusting (burning) proteins. In that scenario you'll go from proteins to CO2, H2O, N2, SO2 etc. You can even go further and try to get everything into just C, H, N etc, but that would require even harsher conditions and I don't even know how to give an example of something like that.

Hope that helps. In regards to people mentioning boiling away micro/macronutrients there are a few things to consider as well. Vitamins are not the same proteins. When boiling things in water, the water soluble vitamins and other nutrients will come out of the cell and go into solution in the water. Then, unless you are drinking the water you boiled stuff in, you will have lost all those nutrients. So there is a bit of truth to that.

When it comes to denaturing proteins, its important to remember that your stomach environment is highly acidic, something like a pH of 2. Most proteins will in fact denature in your stomach. In addition there are enzymes in your intestines which will cut the protein up to make it suitable for transport into blood and throughout the body. Huge proteins are broken down anyway into the amino acids or short peptides of a few amino acids. So the people who talk about denatured dietary proteins being bad for you are a little off their rocker IMO.

Hope this helps.
 
  • #8
Yanick said:
Sorry if I used language that may be a bit over your head.

Here's the takeaway from what I wrote above. I presented my argument somewhat from a top down approach, here it is from a bottom up approach.

atoms -> molecules/amino acids -> peptides -> proteins -> multi-peptide proteins.

The last three exhibit extra levels of organization such as primary, secondary, tertiary and quaternary structure. Briefly, primary structure of a protein is simply just the sequence of amino acids read in a particular direction. Secondary structure refers to how the "string" will arrange itself into things like helices, turns, loops, sheets etc. Tertiary refers to how the secondary structure elements are arranged in space. Finally quaternary structure refers to how two different (or identical) proteins arrange themselves in space if they happen to interact with one another.

Basically you're question is vague because "falling apart" can mean going from a protein, say hemoglobin (which displays all 4 levels of protein structure), to just atoms of C, H, N, O, S etc.

Something like heat denaturation can go all the way to unwinding the protein where it loses its secondary through quaternary structure but still remains a chain of amino acids. You can go further and start cutting up the "string" into individual amino acids (or shorter strings of amino acids), this takes more than just a bit of boiling as you must break peptide (AKA amide) bonds which are pretty strong bonds. Typically this requires something like an enzyme which cuts peptides up known as a peptidase or very harsh conditions such as boiling in concentrated acid for a long time.

You can also go on to say, I want to break each individual amino acid up into smaller molecules, this takes much more effort because bonds like C-C, C-H etc are extremely strong and stable. You can still do something like breaking a protein down where your products are not amino acids but even smaller molecules by combusting (burning) proteins. In that scenario you'll go from proteins to CO2, H2O, N2, SO2 etc. You can even go further and try to get everything into just C, H, N etc, but that would require even harsher conditions and I don't even know how to give an example of something like that.

Hope that helps. In regards to people mentioning boiling away micro/macronutrients there are a few things to consider as well. Vitamins are not the same proteins. When boiling things in water, the water soluble vitamins and other nutrients will come out of the cell and go into solution in the water. Then, unless you are drinking the water you boiled stuff in, you will have lost all those nutrients. So there is a bit of truth to that.

When it comes to denaturing proteins, its important to remember that your stomach environment is highly acidic, something like a pH of 2. Most proteins will in fact denature in your stomach. In addition there are enzymes in your intestines which will cut the protein up to make it suitable for transport into blood and throughout the body. Huge proteins are broken down anyway into the amino acids or short peptides of a few amino acids. So the people who talk about denatured dietary proteins being bad for you are a little off their rocker IMO.

Hope this helps.
That's is very interesting and fairly understandable for me. Thx :)
 

1. What happens to proteins when exposed to exaggerated heat?

Proteins are complex molecules made up of long chains of amino acids. When exposed to exaggerated heat, the heat energy disrupts the bonds between the amino acids, causing the protein to unfold and lose its shape. This process is known as denaturation.

2. Can all proteins withstand exaggerated heat?

No, not all proteins are able to withstand exaggerated heat. Some proteins have a higher tolerance for heat, while others may denature at lower temperatures. The stability of a protein depends on its specific structure and composition.

3. What effect does denaturation have on the function of proteins?

Denaturation can alter the function of proteins by changing their shape. Since proteins are specific to their shape, denaturation can prevent them from performing their normal functions, such as enzymes catalyzing reactions or antibodies binding to antigens.

4. Can denatured proteins return to their original state?

In most cases, denatured proteins cannot return to their original state. Once the bonds between the amino acids are disrupted, it is difficult for the protein to refold back to its original shape. However, some proteins may regain some of their function if the denaturing conditions are reversed quickly.

5. What are some factors that can affect the rate of protein denaturation?

The rate of protein denaturation can be affected by various factors such as temperature, pH, and salt concentration. Higher temperatures and extreme pH levels can denature proteins more quickly, while low temperatures and neutral pH levels may slow down the process.

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