Okay, two articles:
http://www.physorg.com/news134219274.html
and
http://www.physorg.com/news134226755.html
Couple this paragraph from the first:
"That's what the Ohio State chemists find most exciting: the molecule does not maintain only one shape. Depending on its surroundings -- the chemical "nudges" that it receives on the outside -- it will adjust."
with this paragraph from the second:
"Zare's team discovered that as a hydrogen atom passed close to a deuterium molecule, the chemical forces tugged on the nearest of the deuterium atoms in the molecule, pulling it away from the other deuterium atom. But if the tug was not strong enough to break the two deuterium atoms apart, as the hydrogen atom moved farther away its hold on the deuterium atom would weaken. The deuterium atom would eventually slip from its grip and snap back toward the other deuterium atom, initiating an oscillation, or vibration."
So what could be responsible for the multiplicities of protein folding are the "soft" collisions inside the cell between the newly formed peptide chains and ambient elements in the cytoplasm.
Those were interesting articles. Though I would think that protein folding would be more influenced by hydrophobic/hydrophillic interaction with the solvent, in this case he cytosol(assuming mostly water water with some ions) than with a glancing blow with the free proton. I could be wrong though.
Regards,
Caleb
Regards,
Caleb
QUOTE (intropy+Jul 3 2008, 03:19 PM)
Okay, two articles:
http://www.physorg.com/news134219274.html
and
http://www.physorg.com/news134226755.html
Couple this paragraph from the first:
"That's what the Ohio State chemists find most exciting: the molecule does not maintain only one shape. Depending on its surroundings -- the chemical "nudges" that it receives on the outside -- it will adjust."
with this paragraph from the second:
"Zare's team discovered that as a hydrogen atom passed close to a deuterium molecule, the chemical forces tugged on the nearest of the deuterium atoms in the molecule, pulling it away from the other deuterium atom. But if the tug was not strong enough to break the two deuterium atoms apart, as the hydrogen atom moved farther away its hold on the deuterium atom would weaken. The deuterium atom would eventually slip from its grip and snap back toward the other deuterium atom, initiating an oscillation, or vibration."
So what could be responsible for the multiplicities of protein folding are the "soft" collisions inside the cell between the newly formed peptide chains and ambient elements in the cytoplasm.
This can provide a mechanism by which energies on small scales can be magnified by chaotic non-linear physical processes into having larger scale influences.
You can have many possible stable forms the protein can be folded into, but these don't all have to be at the same energy state, though depending upon either initial conditions and/or disturbances (which can be effectively very small) the final stable form reached can be altered significantly. On the other hand, many changes in initial conditions or disturbances during the process have little influence on the state it reaches, so there is a selectivity in how sensitive different influences are in affecting the final form.
This can be a mechanism by which very selective small energies that are not immediately easily observed on larger scales, because of their indirect and chaotic influences, have a large influence on the growth of organic material.
http://www.physorg.com/news134219274.html
and
http://www.physorg.com/news134226755.html
Couple this paragraph from the first:
"That's what the Ohio State chemists find most exciting: the molecule does not maintain only one shape. Depending on its surroundings -- the chemical "nudges" that it receives on the outside -- it will adjust."
with this paragraph from the second:
"Zare's team discovered that as a hydrogen atom passed close to a deuterium molecule, the chemical forces tugged on the nearest of the deuterium atoms in the molecule, pulling it away from the other deuterium atom. But if the tug was not strong enough to break the two deuterium atoms apart, as the hydrogen atom moved farther away its hold on the deuterium atom would weaken. The deuterium atom would eventually slip from its grip and snap back toward the other deuterium atom, initiating an oscillation, or vibration."
So what could be responsible for the multiplicities of protein folding are the "soft" collisions inside the cell between the newly formed peptide chains and ambient elements in the cytoplasm.
This can provide a mechanism by which energies on small scales can be magnified by chaotic non-linear physical processes into having larger scale influences.
You can have many possible stable forms the protein can be folded into, but these don't all have to be at the same energy state, though depending upon either initial conditions and/or disturbances (which can be effectively very small) the final stable form reached can be altered significantly. On the other hand, many changes in initial conditions or disturbances during the process have little influence on the state it reaches, so there is a selectivity in how sensitive different influences are in affecting the final form.
This can be a mechanism by which very selective small energies that are not immediately easily observed on larger scales, because of their indirect and chaotic influences, have a large influence on the growth of organic material.
QUOTE
Though I would think that protein folding would be more influenced by hydrophobic/hydrophillic interaction with the solvent, in this case he cytosol(assuming mostly water water with some ions)
Yeah - I'd read up on that through various sources, starting with wiki. It does sound more plausible (the solvent interaction method), since each protein is made up of many atoms, and the experiment mentioned in the second article was dealing with 3 atoms in total. The complete process, however, is apparently still a mystery. Maybe a more fundamental understanding of the nature of water would clear things up. Do we know the composition of the solvent to an exacting detail?
QUOTE (->
| QUOTE |
| Though I would think that protein folding would be more influenced by hydrophobic/hydrophillic interaction with the solvent, in this case he cytosol(assuming mostly water water with some ions) |
Yeah - I'd read up on that through various sources, starting with wiki. It does sound more plausible (the solvent interaction method), since each protein is made up of many atoms, and the experiment mentioned in the second article was dealing with 3 atoms in total. The complete process, however, is apparently still a mystery. Maybe a more fundamental understanding of the nature of water would clear things up. Do we know the composition of the solvent to an exacting detail?
This can provide a mechanism by which energies on small scales can be magnified by chaotic non-linear physical processes into having larger scale influences.
Kind of what I was thinking. Though I hadn't brought non-linearity into it.
Fast protein folding kinetics -- Schonbrun and Dill 100 (22): 12678 ...
www.pnas.org/cgi/content/full/100/22/12678
Herpes simplex virus type 2 UL14 gene product has heat shock protein ...
jcs.biologists.org/cgi/content/full/115/12/2517
Severe Acute Respiratory Syndrome Coronavirus Protein 6 Accelerates ...
jvi.asm.org/cgi/content/full/79/14/8698
Differential Targeting of Vesicular Stomatitis Virus G Protein and ...
www.jcb.org/cgi/content/full/140/5/1101
Single Amino Acid Mutations Alter the Distribution of Human ...
www.jbc.org/cgi/content/full/281/10/6682
www.pnas.org/cgi/content/full/100/22/12678
Herpes simplex virus type 2 UL14 gene product has heat shock protein ...
jcs.biologists.org/cgi/content/full/115/12/2517
Severe Acute Respiratory Syndrome Coronavirus Protein 6 Accelerates ...
jvi.asm.org/cgi/content/full/79/14/8698
Differential Targeting of Vesicular Stomatitis Virus G Protein and ...
www.jcb.org/cgi/content/full/140/5/1101
Single Amino Acid Mutations Alter the Distribution of Human ...
www.jbc.org/cgi/content/full/281/10/6682
My theory is that proteins don't folds always precisly and they always are in some average state and never completly unfold and at all protein folding don't exist! Just there is big molecules, which some randomly becmoing smaller becouse of they longnest and thus they in such way can do some tricks, becosue are like random snacks, which can grasp somthing and this is seems we basic function of proteins. How proteins making bounce there is another dificult question, which maybe at all don't related with proteins and is harmonical wall of bounce, which protecting from growing into boldness, but into hight... This is stupid, that nature using some very hard interactinos to create human, everything must be much simplier.
QUOTE (DavidD+Jul 4 2008, 05:38 PM)
My theory is that proteins don't folds always precisly and they always are in some average state and never completly unfold and at all protein folding don't exist! Just there is big molecules, which some randomly becmoing smaller becouse of they longnest and thus they in such way can do some tricks, becosue are like random snacks, which can grasp somthing and this is seems we basic function of proteins. How proteins making bounce there is another dificult question, which maybe at all don't related with proteins and is harmonical wall of bounce, which protecting from growing into boldness, but into hight... This is stupid, that nature using some very hard interactinos to create human, everything must be much simplier.
A "yocta-fucktarded monkey-spank" is way too generous as a complimentary description of this ********************************************!
A "yocta-fucktarded monkey-spank" is way too generous as a complimentary description of this ********************************************!
QUOTE (Delia+Jul 4 2008, 05:43 PM)
A "yocta-fucktarded monkey-spank" is way too generous as a complimentary description of this ********************************************!
Have you considered, that though the description of ideas presented by DavidD may not be very precise or technical. At least we can extract some ideas from them, whereas your post contains significantly less useful information than his?
Are you jealous of the content of his post?
Have you considered, that though the description of ideas presented by DavidD may not be very precise or technical. At least we can extract some ideas from them, whereas your post contains significantly less useful information than his?
Are you jealous of the content of his post?
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