Toward understanding driving forces in membrane protein folding.

@article{Hong2014TowardUD,
  title={Toward understanding driving forces in membrane protein folding.},
  author={Heedeok Hong},
  journal={Archives of biochemistry and biophysics},
  year={2014},
  volume={564},
  pages={
          297-313
        }
}
α-Helical membrane proteins are largely composed of nonpolar residues that are embedded in the lipid bilayer. An enigma in the folding of membrane proteins is how a polypeptide chain can be condensed into the compact folded state in the environment where the hydrophobic effect cannot strongly drive molecular interactions. Probably other forces such as van der Waals packing, hydrogen bonding, and weakly polar interactions, which are regarded less important in the folding of water-soluble… CONTINUE READING
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