Congratulations to our award winners for Best Presentation
Arianna Benson (Dr. Dove)
Skeletal muscles require Ca2+ ions to enter the intracellular area for filaments to effect muscle contraction and relaxation (Marieb & Hoehn, 2011). However, as muscles continue to do work, they lose their capacity to achieve a constant force (Gandevia, 1992). This decrease in the maximal force exerted by a muscle is termed muscle fatigue. Conventional wisdom attributed lowered muscle performance to lactic acid build-up, but counter-intuitively, acidosis seems to be beneficial to maintenance of muscle strength (Pedersen, Nielsen, Lamb & Stephenson, 2004). Contemporary research focuses on understanding the ionic interactions that contribute to muscle fatigue (Cairns & Lindinger, 2008). The complexity of these processes presents the need for concrete mathematical models. Expanding on early Hodgkin-Huxley models of nerve cells, researchers have created mathematical models of muscle contractions. Models exist for skeletal muscle function (Dorgan & O’Malley, 1998) and general muscle fatigue (Číhalová, 2010), but a conclusive model of skeletal muscle fatigue has yet to appear. Extensive meta-analysis of existing models and data revealed little measured or measurable data on intracellular calcium concentration. However, models by Looft (2012) and Xia & Frey Law (2008) presented phenomenological models of skeletal muscle fatigue in specific joint regions, providing a model for measurable fatigue.
Aakash Jain (Dr. Elcock)
Recent interest in intrinsically disordered proteins has led to investigation of the conformational behavior of short host-guest GXG peptides (Hagarman, Measey, Mathieu, Schwalbe & Schweitzer¬ Stenner, 2010). GXG molecules are tripeptides that consist of a non-glycine guest residue (labelled as X) flanked by a glycine molecule on each side. Glycine is typically chosen as the neighbor molecule to minimize nearest neighbor interactions (Hagarman, Measey, Mathieu, Schwalbe & Schweitzer¬ Stenner, 2010). Researchers believe that an analysis of the conformational tendencies of such tripeptides can potentially enhance our understanding of protein folding (Graf, Nguyen , Stock & Schwalbe, 2007).
Data from experimental studies have indicated that end groups and pH can significantly affect the conformational properties of these peptides as reflected, for example, in their J-coupling constants. Here we describe our efforts to understand these data using long explicit solvent molecular dynamics (MD) simulations of a variety of GXG peptides. The results highlight the potential benefits and challenges associated with using molecular simulations to interpret experimental data on the conformational behavior of biological molecules.