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Protein folding by a biased Monte Carlo procedure in the dihedral angle space
Author(s) -
Lee B.,
Kurochki.,
Kang g Seok
Publication year - 1996
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.10.1.8566532
Subject(s) - dihedral angle , monte carlo method , folding (dsp implementation) , protein folding , space (punctuation) , statistical physics , function (biology) , process (computing) , computer science , physics , mathematics , molecule , biology , statistics , engineering , quantum mechanics , operating system , evolutionary biology , hydrogen bond , nuclear magnetic resonance , electrical engineering
A straightforward method for predicting the protein structure is to find conformations that have the lowest energy along a chosen folding pathway. One approach in this direction is to produce a large number of structures by varying the dihedral angles of the molecule more or less randomly and then to screen each one using a suitable energy function. This procedure is computationally demanding, but by using a more realistic model, one hopes that the folding behavior one observes in calculations may better mimic the actual folding process in nature. The method is beginning to yield interesting results, thanks to the increase in the computational power but also to the intelligent selection of the folding pathway. This article reviews general features of this method, some important highlights of the particular procedure we used, and some of the more significant results obtained to date in our laboratory. The results are highly encouraging and indicate the direction of future effort that is most likely to be fruitful.—Lee, B., Kurochkina, N., Kang, H. S. Protein folding by a biased Monte Carlo procedure in the dihedral angle space. FASEB J. 10, 119‐125 (1996)