Forces contributing to the conformational stability of proteins.

@article{Pace1996ForcesCT,
  title={Forces contributing to the conformational stability of proteins.},
  author={C. Nick Pace and Bret A Shirley and Marcia McNutt and Ketan S. Gajiwala},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={1996},
  volume={10 1},
  pages={75-83}
}
For 35 years, the prevailing view has been that the hydrophobic effect is the dominant force in protein folding. The importance of hydrogen bonding was always clear, but whether it made a net favorable contribution to protein stability was not. Studies of mutant proteins have improved our understanding of the forces stabilizing proteins. They suggest that hydrogen bonding and the hydrophobic effect make large but comparable contributions to the stability of globular proteins. 

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