scholarly journals Use of time-resolved FRET to validate crystal structure of complement regulatory complex between C3b and factor H (N terminus)

2011 ◽  
Vol 20 (12) ◽  
pp. 2102-2112 ◽  
Author(s):  
Isabell C. Pechtl ◽  
Robert K. Neely ◽  
David T.F. Dryden ◽  
Anita C. Jones ◽  
Paul N. Barlow
Keyword(s):  
Crystal Structure ◽  
Factor H ◽  
Time Resolved ◽  
Use Of Time ◽  
N Terminus ◽  
Regulatory Complex

Determination of Carbon Content in Steel Using Laser-Induced Breakdown Spectroscopy

1992 ◽  
Vol 46 (9) ◽  
pp. 1382-1387 ◽  
Author(s):  
J. A. Aguilera ◽  
C. Aragón ◽  
J. Campos
Keyword(s):  
Carbon Content ◽  
Matrix Effects ◽  
Sample Surface ◽  
Nitrogen Atmosphere ◽  
Laser Induced Breakdown Spectroscopy ◽  
Time Resolved ◽  
Breakdown Spectroscopy ◽  
Use Of Time ◽  
Laser Induced Breakdown

Laser-induced breakdown spectroscopy has been used to determine carbon content in steel. The plasma was formed by focusing a Nd:YAG laser on the sample surface. With the use of time-resolved spectroscopy and generation of the plasma in nitrogen atmosphere, a precision of 1.6% and a detection limit of 65 ppm have been obtained. These values are similar to those of other accurate conventional techniques. Matrix effects for the studied steels are reduced to a small slope difference between the calibration curves for stainless and nonstainless steels.

Insights into the mechanism of host regulation based on the crystal structure of C3b in complex with factor H domains 1–4

2008 ◽  
Vol 45 (16) ◽  
pp. 4098
Author(s):  
Jin Wu ◽  
Bert Janssen ◽  
You-Qiang Wu ◽  
Daniel Ricklin ◽  
John Lambris ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Factor H ◽  
Host Regulation

scholarly journals The biochemical resolving power of fluorescence lifetime imaging

2021 ◽  
Author(s):  
Andrew L. Trinh ◽  
Alessandro Esposito
Keyword(s):  
Fluorescence Lifetime ◽  
Resolving Power ◽  
Fluorescence Lifetime Imaging ◽  
Time Resolved ◽  
Instrument Response Function ◽  
Lifetime Imaging ◽  
Use Of Time ◽  
Single Living Cells ◽  
Microscopy Techniques

AbstractA deeper understanding of spatial resolution in microscopy fostered a technological revolution that is now permitting us to investigate the structure of the cell with nanometer resolution. Although fluorescence microscopy techniques enable scientists to investigate both the structure and biochemistry of the cell, the biochemical resolving power of a microscope is a physical quantity that is not well-defined or studied. To overcome this limitation, we carried out a theoretical investigation of the biochemical resolving power in fluorescence lifetime imaging microscopy, one of the most effective tools to investigate biochemistry in single living cells. With the theoretical analysis of information theory and Monte Carlo simulations, we describe how the ‘biochemical resolving power’ in time-resolved sensing depends on instrument specifications. We unravel common misunderstandings on the role of the instrument response function and provide theoretical insights that have significant practical implications in the design and use of time-resolved instrumentation.

scholarly journals Time-Resolved X-ray Crystal Structure Analysis of Proteins.

1995 ◽  
Vol 35 (6) ◽  
pp. 245-248
Author(s):  
Shin-ichi ADACHI ◽  
Nobuhisa WATANABE
Keyword(s):  
Crystal Structure ◽  
Structure Analysis ◽  
Crystal Structure Analysis ◽  
Time Resolved ◽  
X Ray

Lateral deformations of a crystal of potassium acid phthalate in an external electric field

2021 ◽  
Vol 54 (5) ◽  
pp. 1317-1326
Author(s):  
Arsen Petrenko ◽  
Nataliya Novikova ◽  
Alexander Blagov ◽  
Anton Kulikov ◽  
Yury Pisarevskii ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Electrical Conductivity ◽  
Electric Field ◽  
External Electric Field ◽  
Applied Field ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
Potassium Acid Phthalate ◽  
Acid Phthalate

The anisotropy of deformations in potassium acid phthalate crystals arising under the action of an external electric field up to 1 kV mm−1 applied along the [001] polar axis was studied using X-ray diffraction methods at room temperature. Electrical conductivity was measured and rocking curves for reflections 400, 070 and 004 were obtained by time-resolved X-ray diffractometry in Laue and Bragg geometries. Two saturation processes were observed from the time dependences of the electrical conductivity. A shift in the diffraction peaks and a change in their intensity were found, which indicated a deformation of the crystal structure. Rapid piezoelectric deformation and reversible relaxation-like deformation, kinetically similar to the electrical conductivity of a crystal, were revealed. The deformation depended on the polarity and strength of the applied field. The deformation was more noticeable in the [100] direction and was practically absent in the [001] direction of the applied field. X-ray diffraction analysis revealed a disordered arrangement of potassium atoms, i.e. additional positions and vacancies. The heights of potential barriers between the positions of K+ ions and the paths of their possible migration in the crystal structure of potassium acid phthalate were determined. The data obtained by time-resolved X-ray diffractometry and X-ray structure analysis, along with additional electrophysical measurements, allow the conclusion that the migration of charge carriers (potassium cations) leads to lateral deformation of the crystal structure of potassium phthalate in an external electric field.

scholarly journals Recognition of an α-helical hairpin in P22 large terminase by a synthetic antibody fragment

2020 ◽  
Vol 76 (9) ◽  
pp. 876-888
Author(s):  
Ravi K. Lokareddy ◽  
Ying-Hui Ko ◽  
Nathaniel Hong ◽  
Steven G. Doll ◽  
Marcin Paduch ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Changes ◽  
Recombinant Antibody ◽  
Antibody Fragment ◽  
Genome Packaging ◽  
Synthetic Antibody ◽  
High Affinity ◽  
N Terminus ◽  
Helical Hairpin ◽  
Accessible Surface

The genome-packaging motor of tailed bacteriophages and herpesviruses is a multisubunit protein complex formed by several copies of a large (TerL) and a small (TerS) terminase subunit. The motor assembles transiently at the portal protein vertex of an empty precursor capsid to power the energy-dependent packaging of viral DNA. Both the ATPase and nuclease activities associated with genome packaging reside in TerL. Structural studies of TerL from bacteriophage P22 have been hindered by the conformational flexibility of this enzyme and its susceptibility to proteolysis. Here, an unbiased, synthetic phage-display Fab library was screened and a panel of high-affinity Fabs against P22 TerL were identified. This led to the discovery of a recombinant antibody fragment, Fab4, that binds a 33-amino-acid α-helical hairpin at the N-terminus of TerL with an equilibrium dissociation constant K d of 71.5 nM. A 1.51 Å resolution crystal structure of Fab4 bound to the TerL epitope (TLE) together with a 1.15 Å resolution crystal structure of the unliganded Fab4, which is the highest resolution ever achieved for a Fab, elucidate the principles governing the recognition of this novel helical epitope. TLE adopts two different conformations in the asymmetric unit and buries as much as 1250 Å2 of solvent-accessible surface in Fab4. TLE recognition is primarily mediated by conformational changes in the third complementarity-determining region of the Fab4 heavy chain (CDR H3) that take place upon epitope binding. It is demonstrated that TLE can be introduced genetically at the N-terminus of a target protein, where it retains high-affinity binding to Fab4.

Sign in / Sign up

Export Citation Format

Share Document