Doubly-Balanced Gilbert Cell Down-Conversion Mixer in AMS 0.35  $${\upmu }$$ m SiGe CMOS for Mode-1 MB-OFDM UWB Receivers

Cammarata, Simone; Fieramosca, Giulio; Neri, Bruno; Baronti, Federico; Saponara, Sergio

doi:10.1007/978-3-030-11973-7_43

Cited by 4 publications

(6 citation statements)

References 4 publications

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“…18,22 Direct dissociation from excited electronic states prior to protein unfolding establishes the opportunity for further structural analysis of protein assemblies. 35,45,46 Results for SOD, SA, and TTR are in agreement with previous reports of similar UVPD analyses. 18,22 In the present study, UVPD analysis was expanded to a greater number of native charge states for a more comprehensive understanding of the charge-dependence of UVPD for multimeric complexes.…”

Section: Discussionsupporting

confidence: 91%

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Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes

Sipe

Brodbelt

2019

Phys. Chem. Chem. Phys.

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Section: Discussionsupporting

confidence: 91%

“…The origins of sequence ions with respect to the positions of backbone cleavages are of particular interest because structural insight can be obtained from the fragmentation patterns of native-like proteins or complexes. [45][46][47][48][49]…”

Section: Resultsmentioning

confidence: 99%

Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes

Sipe

Brodbelt

2019

Phys. Chem. Chem. Phys.

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“…These types of plots offer structural insight about macromolecule-ligand complexes; for example, decreases in fragmentation may reflect changes in secondary structure or the presence of ligand interactions that prevent complementary fragment ions from separating after the cleavage of the backbone, thus impeding their detection. 81,82 The binding sites of the silver clusters are determined via the identification of apo and holo ions, not solely via regions of fragmentation suppression. Interestingly, both AgC complexes show a characteristic decrease in sequence coverage at the identified AgC binding locations (Figure 5ac,d) relative to their AgC-free counterparts (Figure 5a,b).…”

Section: Resultsmentioning

confidence: 99%

Footprints of Nanoscale DNA–Silver Cluster Chromophores via Activated-Electron Photodetachment Mass Spectrometry

et al. 2019

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DNA-templated silver clusters (AgC) are fluorescent probes and biosensors whose electronic spectra can be tuned by their DNA hosts. However, the underlying rules that relate DNA sequence and structure to DNA-AgC fluorescence and photophysics are largely empirical. Here, we employ 193 nm activated electron photodetachment (a-EPD) mass spectrometry as a hybrid MS 3 approach to gain structural insight into these nanoscale chromophores. Two DNA-AgC systems are investigated with a 20 nt single-stranded DNA (ssDNA) and a 28 nt hybrid hairpin/single-stranded DNA (hpDNA). Both oligonucleotides template Ag 10 clusters, but the two complexes are distinct chromophores: the former has a violet absorption at 400 nm with no observable emission, while the latter has a blue-green absorption at 490 nm with strong green emission at 550 nm. Via identification of both apo and holo (AgC-containing) sequence ions generated upon a-EPD and mapping areas of sequence dropout, specific DNA regions that encapsulate the AgC are assigned and attributed to the coordination with the DNA nucleobases. These a-EPD footprints are distinct for the two complexes. The ssDNA contacts the cluster via four nucleobases (CCTT) in the central region of the strand, whereas the hpDNA coordinates the cluster via 13 nucleobases (TTCCCGCCTTTTG) in the double-stranded region of the hairpin. This difference is consistent with prior X-ray scattering spectra and suggests that the clusters can adapt to different DNA hosts. More importantly, the a-EPD footprints directly identify the nucleobases that are in direct contact with the AgC. As these contacting nucleobases can tune the electronic structures of the Ag core and protect the AgC from collisional quenching in solution, understanding the DNA-silver contacts within these complexes will facilitate future biosensor designs.

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“…19,20 Comparing the covalent fragmentation patterns of apo and ligand-bound protein complexes can help to locate ligand interaction sites and can provide information on the binding site at the residue level. 19,[21][22][23][24][25][26] However, these techniques are limited to small protein complexes as the chance of signal overlap increases with the number of different fragment ions, making assignments challenging even when using Fourier Transform instruments that provide ultrahigh mass resolution and mass measurement accuracy. 27 Furthermore, partial ligand loss during covalent fragmentation can complicate the analysis for ligand-bound protein complexes and result in the co-occurrence of apo and ligand-bound covalent fragment ion series.…”

mentioning

confidence: 99%

Localization of Protein Complex Bound Ligands by Surface-Induced Dissociation High-Resolution Mass Spectrometry

Büsch

VanAernum

et al. 2018

Anal. Chem.

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Surface-induced dissociation (SID) is a powerful means of deciphering protein complex quaternary structures due to its capability of yielding dissociation products that reflect the native structures of protein complexes in solution. Here we explore the suitability of SID to locate the ligand binding sites in protein complexes. We studied C-reactive protein (CRP) pentamer, which contains a ligand binding site within each subunit, and cholera toxin B (CTB) pentamer, which contains a ligand binding site between each adjacent subunit. SID dissects ligand-bound CRP into subcomplexes with each subunit carrying predominantly one ligand. In contrast, SID of ligandbound CTB results in the generation of subcomplexes with a ligand distribution reflective of two subunits contributing to each ligand binding site. SID thus has potential application in localizing sites of small ligand binding for multisubunit protein-ligand complexes.

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Doubly-Balanced Gilbert Cell Down-Conversion Mixer in AMS 0.35 $${\upmu }$$ m SiGe CMOS for Mode-1 MB-OFDM UWB Receivers

Cited by 4 publications

References 4 publications

Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes

Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes

Footprints of Nanoscale DNA–Silver Cluster Chromophores via Activated-Electron Photodetachment Mass Spectrometry

Localization of Protein Complex Bound Ligands by Surface-Induced Dissociation High-Resolution Mass Spectrometry

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