Docking of a Second Functional Protein Layer to a Streptavidin Matrix on a Solid Support: Studies with a Quartz Crystal Microbalance

1992 ◽  
Vol 31 (8) ◽  
pp. 1087-1090 ◽  
Author(s):  
Wolfgang Müller ◽  
Helmut Ringsdorf ◽  
Peter Suci ◽  
James N. Herron ◽  
Hiroshi Ebato ◽  
...  
Keyword(s):  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Solid Support ◽  
Functional Protein ◽  
Protein Layer

Interaction of Clear Flavor Emulsions Containing Lemon Essential Oils with Lipid Bilayers via a Quartz Crystal Microbalance

2019 ◽  
Vol 25 (6) ◽  
pp. 879-884
Author(s):  
Takahiro Sakai ◽  
Hayato Seki ◽  
Shogo Yoshida ◽  
Hayato Hori ◽  
Hisashi Suzuki ◽  
...  
Keyword(s):  
Essential Oils ◽  
Lipid Bilayers ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal

Effect of Current Distribution on Quartz Crystal Microbalance Measurements

1998 ◽  
Vol 145 (2) ◽  
pp. 492-497 ◽  
Author(s):  
James J. Kelly ◽  
K. M. Anisur Rahman ◽  
Christopher J. Durning ◽  
Alan C. West
Keyword(s):  
Quartz Crystal Microbalance ◽  
Current Distribution ◽  
Quartz Crystal

scholarly journals Unraveling cardiolipin-induced conformational change of cytochrome c through H/D exchange mass spectrometry and quartz crystal microbalance

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sin-Cih Sun ◽  
Hung-Wei Huang ◽  
Yi-Ting Lo ◽  
Min-Chieh Chuang ◽  
Yuan-Hao Howard Hsu
Keyword(s):  
Mass Spectrometry ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Interaction Model ◽  
Moderate Increase ◽  
Exchange Mass Spectrometry ◽  
Mitochondrial Regulation ◽  
Crucial Component ◽  
Drastic Increase ◽  
Hydrogen Deuterium

AbstractCardiolipin (CL), a crucial component in inner mitochondrial membranes, interacts with cytochrome c (cyt c) to form a peroxidase complex for the catalysis of CL oxidation. Such interaction is pivotal to the mitochondrial regulation of apoptosis and is affected by the redox state of cyt c. In the present study, the redox-dependent interaction of cyt c with CL was investigated through amide hydrogen/deuterium exchange coupled with mass spectrometry (HDXMS) and quartz crystal microbalance with dissipation monitoring (QCM-D). Ferrous cyt c exhibited a more compact conformation compared with its ferric form, which was supported by the lower number of deuterons accumulated and the greater amplitude reduction on dissipation. Upon association with CL, ferrous cyt c resulted in a moderate increase in deuteration, whereas the ferric form caused a drastic increase of deuteration, which indicated that CL-bound ferric cyt c formed an extended conformation. These results were consistent with those of the frequency (f) − dissipation (D) experiments, which revealed that ferric cyt c yielded greater values of |ΔD/Δf| within the first minute. Further fragmentation analysis based on HDXMS indicated that the effect of CL binding was considerably different on ferric and ferrous cyt c in the C-helix and the Loop 9–24. In ferric cyt c, CL binding affected Met80 and destabilized His18 interaction with heme, which was not observed with ferrous cyt c. An interaction model was proposed to explain the aforementioned results.

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