TY - JOUR
T1 - Integration of FIRST, FRODA and NMM in a coarse grained method to study Protein Disulphide Isomerase conformational change
AU - Jimenez-Roldan, J.E.
AU - Wells, S.A.
AU - Roemer, R.A.
AU - Freedman, R.B.
PY - 2011/1/1
Y1 - 2011/1/1
N2 - Our simulations of protein motion are based on a rigidity-based coarse graining criteria which is able to identify flexible and constraint regions and on Normal Modes of Motion (NMM) which map out the directions of motion for a given network. The NMM and rigidity constraints are integrated together by the FRODA module to identify large scale conformational changes at low computational cost. In this context we identify the limits for conformational change of a large multi domain protein -Protein Disulphide Isomerase, by re-assessing the principal NMM at intermediate points along a trajectory as the protein moves over the trajectory defined by the initial principal NMM.
AB - Our simulations of protein motion are based on a rigidity-based coarse graining criteria which is able to identify flexible and constraint regions and on Normal Modes of Motion (NMM) which map out the directions of motion for a given network. The NMM and rigidity constraints are integrated together by the FRODA module to identify large scale conformational changes at low computational cost. In this context we identify the limits for conformational change of a large multi domain protein -Protein Disulphide Isomerase, by re-assessing the principal NMM at intermediate points along a trajectory as the protein moves over the trajectory defined by the initial principal NMM.
UR - http://www.scopus.com/inward/record.url?scp=79955901922&partnerID=8YFLogxK
UR - http://dx.doi.org/10.1088/1742-6596/286/1/012002
U2 - 10.1088/1742-6596/286/1/012002
DO - 10.1088/1742-6596/286/1/012002
M3 - Article
AN - SCOPUS:79955901922
SN - 1742-6588
VL - 286
JO - Journal of Physics: Conference Series
JF - Journal of Physics: Conference Series
IS - 1
M1 - 012002
ER -