Fluorescence resonance energy transfer measurements of trapped mass-selected gas-phase ions of biological interest

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Living biological systems are highly complex and their state depends on the interplay of numerous factors that can be difficult to untangle, such as the presence of metal ions, binding partners such as drugs, and even the ever present water molecules. The approach we take is to simplify these systems and study them in a highly controlled environment, the gas phase.  Using our mass spectrometry techniques, a biological molecule of interest such as a protein can be completely isolated (i.e., the environment can be eliminated entirely) to study its intrinsic properties.  Then pieces of the environment (water molecules, metal ions, drugs) can be added back into the system in a controlled manner in order to analyze each effect separately. We analyze the vaporized ions, complexes and clusters using a combination of traditional mass spectrometry techniques and computations as well as laser spectroscopic techniques including fluorescence techniques, newly adapted for gas-phase studies. The research will provide new fundamental information regarding biomolecular structure, function, stability and dynamics and will investigate how the environment affects these properties. We will examine both whole proteins and shorter chains of amino acids that form the smaller structural motifs present in proteins. These studies will provide understanding of protein folding and misfolding, which can cause many devastating diseases (e.g. Alzheimer's and mad cow disease). It will also focus on the development of methods to maintain key interactions during mass spectrometry analysis, such as the binding of drugs to target proteins. This has great potential in the field of drug discovery.