Effective potentials for folding proteins.
A coarse-grained off-lattice model that is not biased in any way to the native state is proposed to fold proteins. To predict the native structure in a reasonable time, the model has included the essential effects of water in an effective potential. Two new ingredients, the dipole-dipole interaction and the local hydrophobic interaction, are introduced and are shown to be as crucial as the hydrogen bonding. The model allows successful folding of the wild-type sequence of protein G and may have provided important hints to the study of protein folding.
Chen
Nan-Yow
NY
Institute of Physics, Academia Sinica, Nankang, Taipei 11529, Taiwan.
Su
Zheng-Yao
ZY
Mou
Chung-Yu
CY
D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008433:Mathematics; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
C029152:G-substrate; D009419:Nerve Tissue Proteins; D014867:Water