Muscle, Movement, and Biophysics
The study of fundamental muscle cell physiology, and how muscles function together to allow action, from contraction of the heart to movement of limbs. Particular research strengths are on understanding the fundamental biophysics of molecular, cellular, and whole-muscle interactions, using quantitative methods to describe the behavior of single molecules as well as movement and posture of humans.
Recent research in this area
- Robert D. Catena & Xu Xu (2016): Hip and knee net joint moments that correlate with success in lateral load transfers over a low friction surface. Ergonomics, DOI: 10.1080/00140139.2016.1154987 PMID: 26883302
- Michael JJ, Gollapudi SK, Chandra M (2016). Interplay between the effects of a Protein Kinase C phosphomimic (T204E) and a dilated cardiomyopathy mutation (K211Δ or R206W) in rat cardiac troponin T blunts the magnitude of muscle length-mediated crossbridge recruitment against the β-myosin heavy chain background. J Muscle Res Cell Motil. 37(3):83-93. doi: 10.1007/s10974-016-9448-2. Epub 2016 Jul 13. PMID: 27411801
- Gollapudi SK, Chandra M (2016). The effect of cardiomyopathy mutation (R97L) in mouse cardiac troponin T on the muscle length-mediated recruitment of crossbridges is modified divergently by α- and β-myosin heavy chain. Arch Biochem Biophys. 601:105-12. doi: 10.1016/j.abb.2016.01.008. Epub 2016 Jan 11. PMCID: PMC4899193
- Hannah C. Pulcastro, Peter O. Awinda, Mei Methawasin, Henk Granzier , Wenji Dong and Bertrand C.W. Tanner (2016). Increased Titin Compliance Reduced Length-Dependent Contraction and Slowed Cross-Bridge Kinetics in Skinned Myocardial Strips from Rbm20ΔRRM Mice. Front. Physiol. http://dx.doi.org/10.3389/fphys.2016.00322 PMCID: PMC4966298
- Fenwick et al. (2016), Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers, Biophysical Journal, http://dx.doi.org/10.1016/j.bpj.2016.09.024 PMID: 26475586