Fragmentation of gold projectiles: From evaporation to total disassembly

We have studied the fragmentation of Au projectiles interacting with targets of C, Al and Cu at an incident energy ofE/A=600 MeV. The employed inverse kinematics allowed a nearly complete detection of projectile fragments with chargeZ≧2. The recorded fragmentation events were sorted according to three observables, the multiplicityM _lp of light charged particles, the largest atomic numberZ _max within an event, and a new observable,Z _bound, representing the sum of the atomic numbersZ of all fragments withZ≧2. Using these observables, the impact parameter dependence of the fragmentation process was investigated. For all three targets, a maximum mean multiplicity of 3 to 4 intermediate mass fragments (IMFs) is observed. The corresponding impact parameters range from central collisions for theC target to increasingly peripheral collisions for the heavier targets. It is found that the correlation between the IMF multiplicity andZ _bound, extending from evaporation type processes (largeZ _bound) to the total disassembly of the projectile (smallZ _bound), is independent of the target nucleus. This universal behaviour may suggest an — at least partial — equilibration of the projectile fragment prior to its decay.     

Acoustic einstein-hopf drag on a bubble

Theoretical results show that the drag on a bubble can be modified by the presence of isotropic, homogeneous, broadband acoustic noise, when the band overlaps the bubble's resonance width. While these results constitute an acoustic analog to the Einstein-Hopf drag on an oscillating dipole in the presence of electromagnetic fluctuations, an important difference is that band-limited acoustic noise can reduce the drag when the lower frequency of the spectrum coincides with the resonant frequency of the bubble. Applications to bubble migration, heat transfer, and acoustophoresis are suggested.     

The Impact of Phosphorylation on Electron Capture Dissociation of Proteins: A Top-Down Perspective

Electron capture dissociation (ECD) is well suited for the characterization of phosphoproteins, with which labile phosphate groups are generally preserved during the fragmentation process. However, the impact of phosphorylation on ECD fragmentation of intact proteins remains unclear. Here, we have performed a systematic investigation of the phosphorylation effect on ECD of intact proteins by comparing the ECD cleavages of mono-phosphorylated α-casein, multi-phosphorylated β-casein, and immunoaffinity-purified phosphorylated cardiac troponin I with those of their unphosphorylated counterparts, respectively. In contrast to phosphopeptides, phosphorylation has significantly reduced deleterious effects on the fragmentation of intact proteins during ECD. On a global scale, the fragmentation patterns are highly comparable between unphosphorylated and phosphorylated precursors under the same ECD conditions, despite a slight decrease in the number of fragment ions observed for the phosphorylated forms. On a local scale, single phosphorylation of intact proteins imposes minimal effects on fragmentation near the phosphorylation sites, but multiple phosphorylations in close proximity result in a significant reduction of ECD bond cleavages.

Open image in new window

Graphical Abstract ?

     

High-Throughput Proteomics Enabled by a Photocleavable Surfactant

Mass spectrometry (MS)-based proteomics provides unprecedented opportunities for understanding the structure and function of proteins in complex biological systems; however, protein solubility and sample preparation before MS remain a bottleneck preventing high-throughput proteomics. Herein, we report a high-throughput bottom-up proteomic method enabled by a newly developed MS-compatible photocleavable surfactant, 4-hexylphenylazosulfonate (Azo) that facilitates robust protein extraction, rapid enzymatic digestion (30 min compared to overnight), and subsequent MS-analysis following UV degradation. Moreover, we developed an Azo-aided bottom-up method for analysis of integral membrane proteins, which are key drug targets and are generally underrepresented in global proteomic studies. Furthermore, we demonstrated the ability of Azo to serve as an “all-in-one” MS-compatible surfactant for both top-down and bottom-up proteomics, with streamlined workflows for high-throughput proteomics amenable to clinical applications.     

High‐Throughput Proteomics Enabled by a Photocleavable Surfactant

Mass spectrometry (MS)‐based proteomics provides unprecedented opportunities for understanding the structure and function of proteins in complex biological systems; however, protein solubility and sample preparation before MS remain a bottleneck preventing high‐throughput proteomics. Herein, we report a high‐throughput bottom‐up proteomic method enabled by a newly developed MS‐compatible photocleavable surfactant, 4‐hexylphenylazosulfonate (Azo) that facilitates robust protein extraction, rapid enzymatic digestion (30 min compared to overnight), and subsequent MS‐analysis following UV degradation. Moreover, we developed an Azo‐aided bottom‐up method for analysis of integral membrane proteins, which are key drug targets and are generally underrepresented in global proteomic studies. Furthermore, we demonstrated the ability of Azo to serve as an “all‐in‐one” MS‐compatible surfactant for both top‐down and bottom‐up proteomics, with streamlined workflows for high‐throughput proteomics amenable to clinical applications.