A General Approach to Kinase Inhibitors



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The biomolecular pair, composed of either two proteins or two nucleic acids, forms noncovalent bonds. In previous studies regarding such pairs, optical tweezers or atomic force microscopy were used; however, such force based techniques have proven to be inconsistent and time consuming. In a study by De Silva, Yao and Xu, force-induced remnant magnetization spectroscopy (FIRMS) was found to be a more efficient technique through its use of acoustic radiation force (ARF) (2014). This study sought to explore the applicability of this technique and quantify the effects of ARF on thee dissociation of noncovalent pairs ï¾— in this instance, DNA ï¾— duplexes, with respect to time and degree of voltage. Such DNA duplexes were prepared over the period of 24 hours and placed directly beneath a piezo disk which generated the ARF. Quantification of the duplexes was achieved through the use of ImageJ, an image-based processing program, and contrasted with images analyzed using atomic magnetometry. The initial hypothesis was that the number of duplexes broken by ARF would remain constant until it eventually plateaued around 90 seconds at 100 and 200 mv. This study adds to the current literature of both fundamental biomolecular research and practical applications due to the noncovalent bonds being the most prevalent intermolecular bonds in biochemistry.