Yesterday PLoS Computational Biology published one of our studies. At PLoS Computational Biology, they have the nice speciality of a ‘friendly abstract’, called the Author Summary. It is supposed to be accessible to a general (educated) audience. As PLoS is all open access, I will shamelessly and righteously copy and paste from our paper:
Dependent on the required physiological function, smooth muscle executes relatively fast contraction-relaxation cycles or maintains long-term contraction. The proteins driving contraction – amongst them actin, tropomyosin, and the contraction-driving myosin motor – can show small changes in the way they are constructed, they can be expressed as different “isoforms”. The isoforms are supposedly tailored to support the specific contraction patterns, but for tropomyosin and actin it is unclear exactly how the isoforms’ differences affect the interaction of actin and myosin that generates the muscle contraction. We measured actin movement outside the cellular environment, focusing on the effects of different isoform combinations of only actin, myosin, and tropomyosin. We found that the actin isoforms cause differences in the mechanical interaction only when tropomyosin is present, not without it. Also, all different actin-tropomyosin combinations affected the mechanical interactions in a different way. In our experiments we could not directly observe the mechanical interactions of actin, tropomyosin, and myosin, so we reconstructed them in a mathematical model. With this model, we could determine in detail how the different actin-tropomyosin combinations caused the differences that we observed in our experiments.
Citation: Hilbert L, Bates G, Roman HN, Blumenthal JL, Zitouni NB, et al. (2013) Molecular Mechanical Differences between Isoforms of Contractile Actin in the Presence of Isoforms of Smooth Muscle Tropomyosin. PLoS Comput Biol 9(10): e1003273. doi:10.1371/journal.pcbi.1003273
The paper has hugely benefited from the reviewers’, editor’s, and staff’s effort, which deserves a special acknowledgement.