Small-Angle X-ray Scattering and Mass Spectrometry Studies of γ-Irradiated C60in Cyclohexane

1996 ◽  
Vol 100 (13) ◽  
pp. 5426-5432 ◽  
Author(s):  
S. J. Henderson ◽  
R. L. Hettich ◽  
R. N. Compton ◽  
G. Bakale
Keyword(s):  
Mass Spectrometry ◽  
Small Angle ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Biophysical Characterization of Cancer-Related Carbonic Anhydrase IX

2020 ◽  
Vol 21 (15) ◽  
pp. 5277
Author(s):  
Katarina Koruza ◽  
A. Briana Murray ◽  
Brian P. Mahon ◽  
Jesse B. Hopkins ◽  
Wolfgang Knecht ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Carbonic Anhydrase ◽  
Small Angle ◽  
Catalytic Domain ◽  
Carbonic Anhydrase Ix ◽  
Biophysical Characterization ◽  
X Ray ◽  
Ca Ix ◽  
X Ray Scattering ◽  
Ray Scattering

Upregulation of carbonic anhydrase IX (CA IX) is associated with several aggressive forms of cancer and promotes metastasis. CA IX is normally constitutively expressed at low levels in selective tissues associated with the gastrointestinal tract, but is significantly upregulated upon hypoxia in cancer. CA IX is a multi-domain protein, consisting of a cytoplasmic region, a single-spanning transmembrane helix, an extracellular CA catalytic domain, and a proteoglycan-like (PG) domain. Considering the important role of CA IX in cancer progression and the presence of the unique PG domain, little information about the PG domain is known. Here, we report biophysical characterization studies to further our knowledge of CA IX. We report the 1.5 Å resolution crystal structure of the wild-type catalytic domain of CA IX as well as small angle X-ray scattering and mass spectrometry of the entire extracellular region. We used matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry to characterize the spontaneous degradation of the CA IX PG domain and confirm that it is only the CA IX catalytic domain that forms crystals. Small angle X-ray scattering analysis of the intact protein indicates that the PG domain is not randomly distributed and adopts a compact distribution of shapes in solution. The observed dynamics of the extracellular domain of CA IX could have physiological relevance, including observed cleavage and shedding of the PG domain.

Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry

2017 ◽  
Vol 86 (1) ◽  
pp. 110-123 ◽  
Author(s):  
Gudrun Rutsdottir ◽  
Morten I. Rasmussen ◽  
Peter Hojrup ◽  
Katja Bernfur ◽  
Cecilia Emanuelsson ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Small Angle ◽  
X Ray ◽  
X Ray Scattering ◽  
Client Proteins ◽  
Ray Scattering

A Revised O2 Reduction Model in Li-O2 Batteries as Revealed by in Situ Small Angle X-Ray Scattering

2019 ◽  
Author(s):  
Christian Prehal ◽  
Aleksej Samojlov ◽  
Manfred Nachtnebel ◽  
Manfred Kriechbaum ◽  
Heinz Amenitsch ◽  
...  
Keyword(s):  
Small Angle ◽  
Wide Angle ◽  
Reduction Mechanism ◽  
Reduction Model ◽  
X Ray ◽  
X Ray Scattering ◽  
O2 Reduction ◽  
Ray Scattering

<b>Here we use in situ small and wide angle X-ray scattering to elucidate unexpected mechanistic insights of the O2 reduction mechanism in Li-O2 batteries.<br></b>

In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

2019 ◽  
Author(s):  
Hao Wu ◽  
Jeffrey Ting ◽  
Siqi Meng ◽  
Matthew Tirrell
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Electrostatic Interactions ◽  
Polyelectrolyte Complex ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Kinetics Of ◽  
Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

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