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Volume 325, number 1,2, 17-22 FEBS 12543 0 1993 Federation of European Biochemical Societies 00145793/93/$6.00
 

Summary: Volume 325, number 1,2, 17-22 FEBS 12543
0 1993 Federation of European Biochemical Societies 00145793/93/$6.00
June 1993
Minireview
Towards protein folding by global energy optimization
Ruben A. Abagyan
European Molecular Biology Laboratory, Meyerhofstraje 1. 6900 Heidelberg, Germany
Received 18 April 1993
Different components of the theoretical protein folding problem are evaluated critically. It is argued that: (i) as a rule, small- and medium-sized
proteins are in the free energy minimum; (ii) long-living metastable states may either appear occasionally with growing protein size, or be selected
by evolution for a specific function; (iii) functions discriminating against incorrect folds would fail if they were used directly in the global
optimization, unless they approximate the true free energy accurately; (iv) surface and electrostatic free energies should be treated separately; (v)
conformational entropy (of side chains in particular) should be taken into account; (vi) Monte Carlo procedures considering all free energy terms
and combining global knowledge-based random moves with local optimization have the largest potential for success.
Protein folding; Global optimization; Free energy; Electrostatics; Solvation; Entropy
1. THE THEORETICAL PROTEIN FOLDING
PROBLEM
Prediction of the native three-dimensional structure
of a protein from the amino acid sequence remains an
unsolved problem despite numerous efforts to solve it

  

Source: Abagyan, Ruben - School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego

 

Collections: Biology and Medicine