Biomolecular interaction analysis sensitivity

Over the past few years we have been developing new mass spectrometric approaches for the rapid, sensitive, and, accurate characterization of proteins. Reported here are some of our findings on the interfacing of Biomolecular Interaction Analysis with mass spectrometry, and the use of enzymatically active - or bioreactive - mass spectrometer probe tips in the characterization of analytes. 

The versatility of the SPR technique has been shown by a vast amount of publications in the past decades the method has matured into a well-accepted analytical tool for the characterization of interfaces and thin films as well as for the sensitive detection of interfacial biomolecular interaction. With a significant input from engineering, SPR has reached a decent signal-to-noise level with a lower limit for a reliable signal detection corresponding to an effective layer of about 0.3 A [6], which is sufficient for most thin film studies. However, the intrinsic label-free characteristic of SPR detection technique still imposes limitation on further sensitivity improvement, especially if the analysis involves small molecules. 

These examples indicate the complexity of the relationships between the properties of liquid water and the model parameters determining the intramolecular and intermolecular interactions of liquid water. Many of the results discussed in this section for liquid water are hard to predict by intuition alone. Water is a comparatively simple system in (bio)molecular modeling, and it is even harder to identify the determinants of the properties of complex biomolecular systems. Sensitivity analysis should thus be a useful tool for sorting out the key contributing factors of interesting biomolecular properties. 

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