does high concentration of Urea break down oligomers? - (Apr/22/2006 )

maybe stupid question but im thinking, urea breaks down the hydrophobic forces so tertiary structure of the protein. But looking at the structure of my protein there are no hydrophobic forces mentioned, only H-bonds, salt bridges, van der waals...in its tertiary as well as quaternary structures. Maybe they are just not mentioned in the paper but they should exist in all proteins... ...sorry im not biochemist....if so then 8M urea will break down my proteins subunits and its tertiary structure right? in another words, will my protein necessarily become a monomer (at least!) after treatment with high conc of urea???

hi,
urea and gu HCl are chiatropic agents, they destroys the three dimensional structure of protein. moreover facilitates the solubilization of protein. to avoid formation of inclusion bodies of expressed protein, generally this purification procedure can be used,
once u purify the protein then u follow another step where u refold the protein for further functional analysis.

gud luk
payeli.

maybe stupid question but im thinking, urea breaks down the hydrophobic forces so tertiary structure of the protein. But looking at the structure of my protein there are no hydrophobic forces mentioned, only H-bonds, salt bridges, van der waals...in its tertiary as well as quaternary structures. Maybe they are just not mentioned in the paper but they should exist in all proteins... ...sorry im not biochemist....if so then 8M urea will break down my proteins subunits and its tertiary structure right? in another words, will my protein necessarily become a monomer (at least!) after treatment with high conc of urea???

a wise man once said to me, " there are no stupid questions, only stupid people!" your question isn't stupid at all.

8M urea will dissociate protein comlexes, so long as they are not connected by di-sulfide linkages. the same will usually apply to the tertiary structure of proteins, though there are a few very tough proteins out there that can mantain nearly native conformation in high concentrations of urea.

most likely, your protein will become a denatured monomer. the consequence of this is that it is unlikely that you'll be able to do activity assays w/ it, as it probably won't renature as well as you'd like.

maybe stupid question but im thinking, urea breaks down the hydrophobic forces so tertiary structure of the protein. But looking at the structure of my protein there are no hydrophobic forces mentioned, only H-bonds, salt bridges, van der waals...in its tertiary as well as quaternary structures. Maybe they are just not mentioned in the paper but they should exist in all proteins... ...sorry im not biochemist....if so then 8M urea will break down my proteins subunits and its tertiary structure right? in another words, will my protein necessarily become a monomer (at least!) after treatment with high conc of urea???

thank you very much for the replies...i wanted to argue with someone that my protein is surely a monomer (at most) after treatment with 8M urea ...but i was not really sure....now I can..