More 2013 Poster Winners: Best Presentation

Congratulations to our award winners for Best Presentation

(Check out other poster award winners here.  Or see all of the posters and abstracts here.)

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.


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