Direct observation of correlated interdomain motion in alcohol dehydrogenase. Export

@article{citeulike:5470470, abstract = {Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spin-echo spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.}, author = {Biehl, Ralf and Hoffmann, Bernd and Monkenbusch, Michael and Falus, Peter and Pr\'{e}ost, Sylvain and Merkel, Rudolf and Richter, Dieter}, citeulike-article-id = {5470470}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/18851497}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=18851497}, day = {26}, issn = {0031-9007}, journal = {Physical review letters}, month = {September}, number = {13}, posted-at = {2009-08-18 21:54:30}, priority = {2}, title = {Direct observation of correlated interdomain motion in alcohol dehydrogenase.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/18851497}, volume = {101}, year = {2008} }

TY - JOUR ID - citeulike:5470470 L3 - citeulike-article-id:5470470 N2 - Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spin-echo spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor. IS - 13 JF - Physical review letters SN - 0031-9007 TI - Direct observation of correlated interdomain motion in alcohol dehydrogenase. VL - 101 AU - Biehl, Ralf AU - Hoffmann, Bernd AU - Monkenbusch, Michael AU - Falus, Peter AU - Préost, Sylvain AU - Merkel, Rudolf AU - Richter, Dieter PY - 2008/09/26/ UR - http://view.ncbi.nlm.nih.gov/pubmed/18851497 ER -