Using a new method called steric trapping, researchers have been able
to elucidate the complex process of protein folding. Folding errors
result in proteins clumping together; formation of plaques; such as
those found in Parkinson’s disease and cystic fibrosis; and cell
degeneratation.
Heedeok Hong, a chemist at Michigan State University (MSU), explained, “Our novel tool set can potentially be applied to analyze how disease mutations impact the structural and functional integrity of pathologically important membrane proteins. This knowledge will ultimately help in designing treatments that can stabilize defective membrane proteins for their optimal function.”
The team focused on membrane proteins because about 30% of all proteins reside in this oily layer that encapsulates cells. Using the new procedure, the researchers attached two small molecular tags to a protein in its folded form, and then added bulky objects that bind the tags. The large attachments unravel the protein to its unfolded state.
Steric trapping can test the stability of membrane proteins, show what unfolded membrane proteins look like and reveal how individual amino acids that are building a protein work together to maintain its folded shape.
“Using this novel tag-binding system … our team was able to observe and test membrane proteins without disturbing their native environment,” Hong said. “Controlling folding and unfolding while keeping their native membrane environment has been one of the major methodological hurdles to solve the membrane protein folding problem.”
source:
http://www.americanlaboratory.com/184881-Steric-Trapping-Sheds-Light-on-Protein-Folding/
more here:
http://msutoday.msu.edu/news/2016/msu-tackles-mystery-of-protein-folding/
Heedeok Hong, a chemist at Michigan State University (MSU), explained, “Our novel tool set can potentially be applied to analyze how disease mutations impact the structural and functional integrity of pathologically important membrane proteins. This knowledge will ultimately help in designing treatments that can stabilize defective membrane proteins for their optimal function.”
The team focused on membrane proteins because about 30% of all proteins reside in this oily layer that encapsulates cells. Using the new procedure, the researchers attached two small molecular tags to a protein in its folded form, and then added bulky objects that bind the tags. The large attachments unravel the protein to its unfolded state.
Steric trapping can test the stability of membrane proteins, show what unfolded membrane proteins look like and reveal how individual amino acids that are building a protein work together to maintain its folded shape.
“Using this novel tag-binding system … our team was able to observe and test membrane proteins without disturbing their native environment,” Hong said. “Controlling folding and unfolding while keeping their native membrane environment has been one of the major methodological hurdles to solve the membrane protein folding problem.”
source:
http://www.americanlaboratory.com/184881-Steric-Trapping-Sheds-Light-on-Protein-Folding/
more here:
http://msutoday.msu.edu/news/2016/msu-tackles-mystery-of-protein-folding/
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