Unimolecular Dissociation Kinetics of Benzene Cluster Ions

1996 ◽  
Vol 69 (4) ◽  
pp. 915-924 ◽  
Author(s):  
Kazuhiko Ohashi ◽  
Kei Adachi ◽  
Nobuyuki Nishi
2013 ◽  
Vol 117 (46) ◽  
pp. 11924-11932 ◽  
Author(s):  
Jongcheol Seo ◽  
Seung-Joon Kim ◽  
Seung Koo Shin

ChemInform ◽  
1988 ◽  
Vol 19 (43) ◽  
Author(s):  
A. KIERMEIER ◽  
B. ERNSTBERGER ◽  
H. J. NEUSSER ◽  
E. W. SCHLAG

1988 ◽  
Vol 92 (13) ◽  
pp. 3785-3789 ◽  
Author(s):  
A. Kiermeier ◽  
B. Ernstberger ◽  
H. J. Neusser ◽  
E. W. Schlag

2005 ◽  
Vol 11 (2) ◽  
pp. 231-242 ◽  
Author(s):  
Lianming Wu ◽  
R. Graham Cooks

The fixed-ligand version of the kinetic method has been used for chiral and for isomeric analysis by studying the dissociation kinetics of transition metal-bound trimeric cluster ions ([(MII + Lfixed – H)(ref*)(An)]+, where MII is a transition metal, Lfixed is a fixed (non-dissociating) ligand, ref* is a reference ligand and An is the analyte. The trimeric cluster ions are readily generated by electrospray ionization (ESI) or sonic spray ionization (SSI). The size of the fixed ligand, L-Phe–Gly–L-Phe–Gly, is chosen based on previous results but with the inclusion of aromatic functionality to increase chiral recognition. Improved chiral/isomeric differentiation results from enhanced chiral/isomeric interactions (metal–ligand and ligand–ligand) due to the fixed ligand. As shown in the cases of chiral dipeptides (D-Ala–D-Ala/L-Ala–L-Ala), sugars (D/L-glucose, D/L-mannose) and isomeric tetrapeptides (L-Ala–Gly–Gly–Gly/Gly–Gly–Gly–L-Ala), improved chiral/isomeric discrimination by factors from three to six were obtained by the fixed ligand procedure. Chiral recognition is independent of the concentrations of the analyte, the reference ligand, the fixed ligand and the transition metal salt, a great advantage for practical applications. In addition to increased chiral distinction, the simplified dissociation kinetics also contribute to improved accuracy in chiral quantification, in comparison with data obtained by investigating the dissociation kinetics of simple trimeric cluster ions [MII(ref*)2(An) – H]+. Accurate determination of enantiomeric excess ( ee) is demonstrated by enantiomeric quantification of D-Ala–D-Ala/L-Ala–L-Ala down to 2% ee. Both ESI and SSI allow chiral quantification with similar accuracies. The performance of chiral analysis experiments is not limited to ion trapping devices such as quadrupole ion trap mass spectrometers; a hybrid quadrupole-time of flight (Q-ToF) mass spectrometer is shown to provide an alternative choice. The fixed-ligand kinetic method is not restricted to any particular kinds of isomers and, hence, represents a general procedure for improving molecular recognition and chiral analysis in the gas phase.


1988 ◽  
Vol 92 (3) ◽  
pp. 437-440 ◽  
Author(s):  
A. Kiermeier ◽  
B. Ernstberger ◽  
H. J. Neusser ◽  
E. W. Schlag

Nano Research ◽  
2021 ◽  
Author(s):  
Yishang Wu ◽  
Yufang Xie ◽  
Shuwen Niu ◽  
Yipeng Zang ◽  
Jinyan Cai ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Betty Ha ◽  
Kevin P. Larsen ◽  
Jingji Zhang ◽  
Ziao Fu ◽  
Elizabeth Montabana ◽  
...  

AbstractReverse transcription of the HIV-1 viral RNA genome (vRNA) is an integral step in virus replication. Upon viral entry, HIV-1 reverse transcriptase (RT) initiates from a host tRNALys3 primer bound to the vRNA genome and is the target of key antivirals, such as non-nucleoside reverse transcriptase inhibitors (NNRTIs). Initiation proceeds slowly with discrete pausing events along the vRNA template. Despite prior medium-resolution structural characterization of reverse transcriptase initiation complexes (RTICs), higher-resolution structures of the RTIC are needed to understand the molecular mechanisms that underlie initiation. Here we report cryo-EM structures of the core RTIC, RTIC–nevirapine, and RTIC–efavirenz complexes at 2.8, 3.1, and 2.9 Å, respectively. In combination with biochemical studies, these data suggest a basis for rapid dissociation kinetics of RT from the vRNA–tRNALys3 initiation complex and reveal a specific structural mechanism of nucleic acid conformational stabilization during initiation. Finally, our results show that NNRTIs inhibit the RTIC and exacerbate discrete pausing during early reverse transcription.


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