~ Archive for Science news ~
Update on Zvonimir Dogic’s lab
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The PhysicsWeb article “Doing Physics with Bacteria” highlights the
work of Rowland’s Zvonimir Dogic, who studies phase transitions of
bacterial flagellar filaments in their latest paper.
Paper by Trapped Ion Dynamics Group
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Rowland’s Trapped Ion Dynamics Group
published a paper on electron diffraction of silver clusters in an ion trap. (Harvard affiliates enter here.)
On false research findings
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From PLoS Medicine: “There is increasing concern that most current
published research findings are false. The probability that a research
claim is true may depend on study power and bias, the number of other
studies on the same question, and, importantly, the ratio of true to no
relationships among the relationships probed in each scientific field.
In this framework, a research finding is less likely to be true when
the studies conducted in a field are smaller; when effect sizes are
smaller; when there is a greater number and lesser preselection of
tested relationships; where there is greater flexibility in designs,
definitions, outcomes, and analytical modes; when there is greater
financial and other interest and prejudice; and when more teams are
involved in a scientific field in chase of statistical significance.
Simulations show that for most study designs and settings, it is more
likely for a research claim to be false than true. Moreover, for many
current scientific fields, claimed research findings may often be
simply accurate measures of the prevailing bias.” (Sources: Daypop,
ResourceShelf)
On nonlinear optics of chiral molecules
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(Harvard affiliates follow this link. ) Rowland Junior Fellow Peer Fischer,
who studies “all things chiral,” has published a review article on
applying nonlinear optics to chiral molecules. (Source: Peer
Fischer)
Paper by Single Molecule Biophysics Group
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Members of Rowland’s Single Molecule Biophysics Group, in collaboration
with other researchers at Harvard and Urbana-Champaign, report on
the dynamics of single DNA molecules within a narrow protein
pore. (Harvard users follow this link.)