Fast-scan cyclic voltammetry (FSCV) can detect small changes in dopamine concentration; however, measurements are typically limited to scan repetition frequencies of 10 Hz. Dopamine oxidation at carbon-fiber microelectrodes (CFMEs) is dependent on dopamine adsorption, and increasing the frequency of FSCV scan repetitions decreases the oxidation current, because the time for adsorption is decreased. Using a commercially available carbon nanotube yarn, we characterized carbon nanotube yarn microelectrodes (CNTYMEs) for high-speed measurements with FSCV. For dopamine, CNTYMEs have a significantly lower ΔEp than CFMEs, a limit of detection of 10 ± 0.8 nM, and a linear response to 25 μM. Unlike CFMEs, the oxidation current of dopamine at CNTYMEs is independent of scan repetition frequency. At a scan rate of 2000 V/s, dopamine can be detected, without any loss in sensitivity, with scan frequencies up to 500 Hz, resulting in a temporal response that is four times faster than CFMEs. While the oxidation current is adsorption-controlled at both CFMEs and CNTYMEs, the adsorption and desorption kinetics differ. The desorption coefficient of dopamine-o-quinone (DOQ), the oxidation product of dopamine, is an order of magnitude larger than that of dopamine at CFMEs; thus, DOQ desorbs from the electrode and can diffuse away. At CNTYMEs, the rates of desorption for dopamine and dopamine-o-quinone are about equal, resulting in current that is independent of scan repetition frequency. Thus, there is no compromise with CNTYMEs: high sensitivity, high sampling frequency, and high temporal resolution can be achieved simultaneously. Therefore, CNTYMEs are attractive for high-speed applications.

Described herein are several unique analytical applications utilizing mass spectrometry and the selective modification of the free thiol form of cysteine in both peptides and proteins by various quinones. This simple modification can be used to quantify the number of free or disulfide bound cysteines in a protein. In addition, quinone modification can also be used to easily probe the solvent accessibility of cysteine residues, which provides information about protein structure or folding state. Furthermore, the chromophoric properties of the quinone moiety can be leveraged for site specific photodissociation of the backbone. The photodissociation reveals both the presence and location of modified cysteine residues. For example, cleavage of the protein backbone of α-hemoglobin is observed selectively at a single cysteine out of 140 residues in the whole protein. This selective backbone fragmentation is accompanied by a parent ion mass loss, which is unique to the modifying quinone. When combined, this information can be used to determine both the presence and site of modification generated by naturally occurring molecules, such as dopamine, which can harness quinone chemistry to modify proteins.