@misc{JavanainenMartinezSearaMetzleretal.2017, author = {Javanainen, Matti and Martinez-Seara, Hector and Metzler, Ralf and Vattulainen, Ilpo Tapio}, title = {Diffusion of Proteins and Lipids in Protein-Rich Membranesa}, series = {Biophysical journal}, volume = {114}, journal = {Biophysical journal}, number = {3}, publisher = {Cell Press}, address = {Cambridge}, issn = {0006-3495}, doi = {10.1016/j.bpj.2017.11.3009}, pages = {551A -- 551A}, year = {2017}, language = {en} } @misc{GudowskaNowakLindenbergMetzler2017, author = {Gudowska-Nowak, Ewa and Lindenberg, Katja and Metzler, Ralf}, title = {Preface: Marian Smoluchowski's 1916 paper—a century of inspiration}, series = {Journal of physics : A, Mathematical and theoretical}, volume = {50}, journal = {Journal of physics : A, Mathematical and theoretical}, number = {38}, publisher = {IOP Publ. Ltd.}, address = {Bristol}, issn = {1751-8113}, doi = {10.1088/1751-8121/aa8529}, pages = {8}, year = {2017}, language = {en} } @misc{Metzler2017, author = {Metzler, Ralf}, title = {Gaussianity Fair}, series = {Biophysical journal}, volume = {112}, journal = {Biophysical journal}, number = {3}, publisher = {Cell Press}, address = {Cambridge}, issn = {0006-3495}, doi = {10.1016/j.bpj.2016.12.019}, pages = {413 -- 415}, year = {2017}, language = {en} } @misc{Metzler2017, author = {Metzler, Ralf}, title = {Anomalous Diffusion in Membranes and the Cytoplasm of Biological Cells}, series = {Biophysical journal}, volume = {112}, journal = {Biophysical journal}, number = {3}, publisher = {Cell Press}, address = {Cambridge}, issn = {0006-3495}, doi = {10.1016/j.bpj.2016.11.2577}, pages = {476A -- 476A}, year = {2017}, language = {en} } @misc{BarkaiGariniMetzler2013, author = {Barkai, Eli and Garini, Yuval and Metzler, Ralf}, title = {Electrostatic effects in living cells Reply}, series = {PHYSICS TODAY}, volume = {66}, journal = {PHYSICS TODAY}, number = {7}, publisher = {AMER INST PHYSICS}, address = {MELVILLE}, issn = {0031-9228}, pages = {11 -- 11}, year = {2013}, language = {en} } @misc{TalukderSenChakrabortietal.2014, author = {Talukder, Srijeeta and Sen, Shrabani and Chakraborti, Prantik and Metzler, Ralf and Banik, Suman K. and Chaudhury, Pinaki}, title = {Breathing dynamics based parameter sensitivity analysis of hetero-polymeric DNA}, series = {The journal of chemical physics : bridges a gap between journals of physics and journals of chemistr}, volume = {140}, journal = {The journal of chemical physics : bridges a gap between journals of physics and journals of chemistr}, number = {14}, publisher = {American Institute of Physics}, address = {Melville}, issn = {0021-9606}, doi = {10.1063/1.4871297}, pages = {1}, year = {2014}, abstract = {We study the parameter sensitivity of hetero-polymeric DNA within the purview of DNA breathing dynamics. The degree of correlation between the mean bubble size and the model parameters is estimated for this purpose for three different DNA sequences. The analysis leads us to a better understanding of the sequence dependent nature of the breathing dynamics of hetero-polymeric DNA. Out of the 14 model parameters for DNA stability in the statistical Poland-Scheraga approach, the hydrogen bond interaction epsilon(hb)(AT) for an AT base pair and the ring factor. turn out to be the most sensitive parameters. In addition, the stacking interaction epsilon(st)(TA-TA) for an TA-TA nearest neighbor pair of base-pairs is found to be the most sensitive one among all stacking interactions. Moreover, we also establish that the nature of stacking interaction has a deciding effect on the DNA breathing dynamics, not the number of times a particular stacking interaction appears in a sequence. We show that the sensitivity analysis can be used as an effective measure to guide a stochastic optimization technique to find the kinetic rate constants related to the dynamics as opposed to the case where the rate constants are measured using the conventional unbiased way of optimization.}, language = {en} } @misc{Metzler2016, author = {Metzler, Ralf}, title = {PROTEIN PHYSICS Forever ageing}, series = {Nature physics}, volume = {12}, journal = {Nature physics}, publisher = {Nature Publ. Group}, address = {London}, issn = {1745-2473}, doi = {10.1038/nphys3585}, pages = {113 -- 114}, year = {2016}, abstract = {Single-molecule techniques have long given us insight into the motion and interactions of individual molecules. But simulations now show that the dynamics inside single proteins is not as simple as we thought — and that proteins are forever changing.}, language = {en} }