Chemical Research in Chinese Universities ›› 1994, Vol. 10 ›› Issue (2): 134-140.

• Articles • Previous Articles     Next Articles

Recognition of Protein Native Folds Using a Continuous Potential Function

WANG Yu-hong, LU Zhi-bin, LI Wei   

  1. Department of Molecular Biology, Jilin University, Changchun, 130023
  • Received:1993-07-03 Online:1994-04-24 Published:2011-08-17
  • Supported by:

    Supported by the National Natural Science Houndation of China(39270182) and US National Science Foundation(INT-9107818).

Abstract: We report a simple continuous potential function that can recognize proteinchains' native folds from tens of thousands of alternative ones.Empirical parame-ters for this potential function were obtained by a neural network learning oversamples generated from PDBstructural data.Hydrophobic interactions were foundto be mainly responsible for stabilization of the protein' s native fold.The inter-chain interaction was found indispensable in stabilizing some protein chains' nativeconformation.

Key words: Recognition, Protein native fold, Function