Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry

Ly, Tony; Julian, Ryan R.

doi:10.1016/j.jasms.2008.07.006

Cited by 46 publications

(44 citation statements)

References 64 publications

(60 reference statements)

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“…Indeed, as shown by CD in Figure 1 the protein unfolded after the volume of the solution was significantly reduced, presumably due to concentration of DMSO. In fact, if it is assumed that only water is lost, then the percent DMSO where denaturation occurs is in good agreement with previous experiments [22,23]. The point here is that the solution composition in ESI droplets is most likely evolving with time as evaporation and ionization occur.…”

Section: Timescalesupporting

confidence: 89%

“…Calmodulin has been examined frequently by mass spectrometry, [21,22] but one experiment is particularly relevant here. [23] Selective noncovalent adduct protein probing (SNAPP) is a mass spectrometry based method that utilizes 18-crown-6 ether (18C6) to examine protein structure. 18C6 forms stable noncovalent adducts with proteins in the gas phase when electrosprayed under gentle conditions.…”

Section: The Interesting Case Of Calmodulinmentioning

confidence: 99%

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Reflections on Charge State Distributions, Protein Structure, and the Mystical Mechanism of Electrospray Ionization

Hamdy

Julian

2011

J. Am. Soc. Mass Spectrom.

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The connection between charge state distributions, protein structure, and mechanistic details of electrospray are discussed in relation to the emerging field of gas phase structural biology. Comparisons are drawn with the established area of enzymatic catalysis in organic solvents, which shares many similar challenges. Charge solvation emerges as a dominant force in both systems that must be dealt with to enable kinetic trapping of native structures in foreign environments. Potential methods for mediating unfavorable charge solvation effects are discussed and, ironically, do not include partial solvation by water. The importance of timescale in relation to the evolution of protein structure during the process of electrospray ionization is discussed. Finally several prospects for future endeavors are highlighted.

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Section: Timescalesupporting

confidence: 89%

Section: The Interesting Case Of Calmodulinmentioning

confidence: 99%

Reflections on Charge State Distributions, Protein Structure, and the Mystical Mechanism of Electrospray Ionization

Hamdy

Julian

2011

J. Am. Soc. Mass Spectrom.

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“…In this context, the three-fold symmetry axis of 18-crown-6 (18c6) (i.e., symmetry group D 3d ) and its cavity size offer an attractive binding pocket for NH 3 + , forming three strong N−H + ···O hydrogen-bonding interactions. 3,6,24, 25 Julian and co-workers have employed crown ethers as a structural probe of proteins in the selective noncovalent adduct protein probing (SNAPP) approach, 9,26 given the high binding affinity of 18c6 for the lysine side chains. Julian, as well as Brodbelt, have also employed crown ethers as UV chromophores to induce photodissociation of noncovalently bound crown ether complexes.…”

Section: ■ Introductionmentioning

confidence: 99%

Crown Complexation of Protonated Amino Acids: Influence on IRMPD Spectra

et al. 2012

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We report infrared multiple photon dissociation (IRMPD) spectra for a series of crown-adducted, protonated amino acids, generated by electrospray ionization. The tight chelation of 18-crown-6 on the protonated NH(3)(+) moiety results in a considerable red shift of the NH(3)(+) stretch modes, notably the antisymmetric NH(3)(+) stretch. This is rationalized by a distortion of the NH(3)(+) normal mode potential energy surface, as verified by quantum chemical calculations. On the other hand, the local oscillator modes, such as the carboxylic acid OH stretch, indole NH stretch, and phenol OH stretches, remain well-resolved and are subject to minor and predictable blue shifts of 5-15 cm(-1). Other chemically diagnostic modes, such as the guanidine NH stretch and alcohol OH stretches, also have discernible band positions. Crucially, some of these diagnostic band positions have little to no overlap with one another and can hence be readily distinguished. In addition, the complexes are often found to efficiently photodissociate by neutral loss of 18-crown-6, particularly for higher-basicity amino acids. This in principle opens the door on multiplexing the IRMPD experiment, where the IR spectra of multiple precursors are recorded simultaneously.

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“…This agrees well with another study where CE complexes with ubiquitin lysine-to-asparagine mutants were analysed via selective noncovalent adduct protein probing mass spectrometry (SNAPP-MS). [40][41][42] Here, the authors investigate the changing adduct distribution in mass spectra for mutants with only one lysine replaced in the sequence and reveal that intramolecular interactions, such as salt bridges and hydrogen bonds, can hamper the coordination of 18C6 to protonated lysine residues. 29 …”

Section: Ion Mobility-mass Spectrometry Experimentsmentioning

confidence: 99%

Gas-phase microsolvation of ubiquitin: investigation of crown ether complexation sites using ion mobility-mass spectrometry

Göth

Lermyte

Schmitt

et al. 2016

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In this study the gas-phase structure of ubiquitin and its lysine-to-arginine mutants was investigated using ion mobility-mass spectrometry (IM-MS) and electron transfer dissociation-mass spectrometry (ETD-MS). Crown ether molecules were attached to positive charge sites of the proteins and the resulting noncovalent complexes were analysed. Collision induced dissociation (CID) experiments revealed relative energy differences between the wild type and the mutant crown-ether complexes. ETD-MS experiments were performed to identify the crown ether binding sites. Although not all of the binding sites could be revealed, the data confirm that the first crown ether is able to bind to the N-terminus. IM-MS experiments show a more compact structure for specific charge states of wild type ubiquitin when crown ethers are attached. However, data on ubiquitin mutants reveal that only specific lysine residues contribute to the effect of charge microsolvation. A compaction is only observed for one of the investigated mutants, in which the lysine has no proximate interaction partner. On the other hand when the lysine residues are involved in salt bridges, attachment of crown ethers has little effect on the structure.

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Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry

Cited by 46 publications

References 64 publications

Reflections on Charge State Distributions, Protein Structure, and the Mystical Mechanism of Electrospray Ionization

Reflections on Charge State Distributions, Protein Structure, and the Mystical Mechanism of Electrospray Ionization

Crown Complexation of Protonated Amino Acids: Influence on IRMPD Spectra

Gas-phase microsolvation of ubiquitin: investigation of crown ether complexation sites using ion mobility-mass spectrometry

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