Protein folding by a biased Monte Carlo procedure in the dihedral angle space. Export

@article{citeulike:2416591, abstract = {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.}, address = {Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-4255, USA.}, author = {Lee, B. and Kurochkina, N. and Kang, H. S.}, citeulike-article-id = {2416591}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/8566532}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=8566532}, issn = {0892-6638}, journal = {FASEB J}, keywords = {folding, protein}, month = {January}, number = {1}, pages = {119--125}, posted-at = {2008-02-23 03:31:25}, priority = {2}, title = {Protein folding by a biased Monte Carlo procedure in the dihedral angle space.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8566532}, volume = {10}, year = {1996} }

TY - JOUR ID - citeulike:2416591 L3 - citeulike-article-id:2416591 N2 - 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. IS - 1 JF - FASEB J SN - 0892-6638 AD - Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-4255, USA. EP - 125 TI - Protein folding by a biased Monte Carlo procedure in the dihedral angle space. VL - 10 SP - 119 KW - folding KW - protein AU - Lee, B AU - Kurochkina, N AU - Kang, HS PY - 1996/01// UR - http://view.ncbi.nlm.nih.gov/pubmed/8566532 ER -