Mendonca, Matheus R. deRizzi, Leandro G.Contessoto, Vinicius [UNESP]Leite, Vitor Barbanti Pereira [UNESP]Alves, Nelson A.2014-12-032014-12-032014-01-01Proteins-structure Function And Bioinformatics. Hoboken: Wiley-blackwell, v. 82, n. 1, p. 119-129, 2014.0887-3585http://hdl.handle.net/11449/112900A number of studies have demonstrated that simple elastic network models can reproduce experimental B-factors, providing insights into the structure-function properties of proteins. Here, we report a study on how to improve an elastic network model and explore its performance by predicting the experimental B-factors. Elastic network models are built on the experimental C coordinates, and they only take the pairs of C atoms within a given cutoff distance r(c) into account. These models describe the interactions by elastic springs with the same force constant. We have developed a method based on numerical simulations with a simple coarse-grained force field, to attribute weights to these spring constants. This method considers the time that two C atoms remain connected in the network during partial unfolding, establishing a means of measuring the strength of each link. We examined two different coarse-grained force fields and explored the computation of these weights by unfolding the native structures. Proteins 2014; 82:119-129. (c) 2013 Wiley Periodicals, Inc.119-129engnormal mode analysisGNMpfGNMWCNB-factorvibrational dynamicsArtigo10.1002/prot.24381WOS:000328090900011Acesso aberto0500034174785796