scholarly journals X-ray Crystallographic and Steady State Fluorescence Characterization of the Protein Dynamics of Yeast Polyadenylate Polymerase

2007 ◽  
Vol 366 (5) ◽  
pp. 1401-1415 ◽  
Author(s):  
Paul B. Balbo ◽  
Joe Toth ◽  
Andrew Bohm
Keyword(s):  
Steady State ◽  
Protein Dynamics ◽  
X Ray ◽  
Steady State Fluorescence

The Steady-State and Decay Characteristics of Protein Tryptophan Fluorescence from Algae

1988 ◽  
Vol 42 (8) ◽  
pp. 1405-1412 ◽  
Author(s):  
M. Baek ◽  
W. H. Nelson ◽  
P. E. Hargraves ◽  
J. F. Tanguay ◽  
S. L. Suib
Keyword(s):  
Steady State ◽  
Tryptophan Fluorescence ◽  
Fluorescence Decay ◽  
Direct Application ◽  
Fluorescence Lifetimes ◽  
Bacterial Protein ◽  
Steady State Fluorescence ◽  
Tryptophan Residues ◽  
Rapid Characterization

The intrinsic steady-state fluorescence due to tryptophan has been obtained from monospecific cultures of fourteen plankton algae of various genera. Fluorescence decay profiles of protein tryptophan residues were obtained for eight marine plankton algae. Each organism exhibits a strong maximum in its emission spectrum at 320–340 nm when excited at 290 nm. Iodide quenching and denaturization experiments with 8 M urea provide strong evidence for the assignment of the 320–340 nm fluorescence to protein tryptophan. Most importantly, the decay of this bacterial protein tryptophan fluorescence has been described. The observation that characteristic protein-tryptophan fluorescence lifetimes have been obtained for each organism suggests that measurements of fluorescence lifetimes may be helpful in the rapid characterization of algae. Direct application will likely be found in combination with the measurement of other luminescence parameters.

scholarly journals Diagnostic Characterization of Laser-Irradiated dot Targets

1988 ◽  
Vol 102 ◽  
pp. 375-378
Author(s):  
G. Charatis ◽  
G.E. Busch ◽  
B.K.F. Young ◽  
R.E. Stewart
Keyword(s):  
Steady State ◽  
Spectral Line ◽  
Holographic Interferometry ◽  
Line Ratio ◽  
X Ray ◽  
Preliminary Results ◽  
Spatial Gradients ◽  
Simultaneous Measurements ◽  
Series Of Experiments

AbstractWe have conducted a series of experiments at the KMS CHROMA facility using dot spectroscopy techniques to characterize uncertainties associated with spectral line ratio models commonly applied in determining electron temperatures and densities. Temperatures determined from the slope of the H-like free-bound continuum and densities via holographic interferometry, are compared to line ratio methods. Dot targets of (typically 100µmD Mg or Al) are irradiated with 2 to 40 × 1013W/cm2of 0.53µmlight. Time and spatial gradients are resolved using 4 diagnostics: a 4-frame holographic interferometer, an x-ray streak crystal spectrograph with a spatial imaging slit, a framing crystal x-ray spectrometer, and a conventional space-resolved time-integrating crystal spectrograph used for survey and calibration purposes. Preliminary results indicate the ionization distribution of these laser produced plasmas is not steady-state which plays an important role in measuring the temperature and and density. Electron temperatures derived from line-ratio techniques, assuming steady state conditions, disagree dramatically from simultaneous measurements using the slope of the H-like continuum. Electron densities using He-like triplet to singlet line ratios also differ from densities measured interferometrically.

Steady—state fluorescence quenching as a tool to study protein dynamics

1989 ◽  
Vol 42 ◽  
pp. 45-58 ◽  
Author(s):  
B. Somogyi ◽  
Zs. Lakos ◽  
S. Damjanovich ◽  
A. Rosenberg
Keyword(s):  
Steady State ◽  
Fluorescence Quenching ◽  
Protein Dynamics ◽  
Steady State Fluorescence

Preparation and Characterization of Konjac Glucomannan Gel

2011 ◽  
Vol 117-119 ◽  
pp. 1374-1376 ◽  
Author(s):  
Dong Ying Xu ◽  
Zheng Fu Liao ◽  
Hui Wang
Keyword(s):  
Fourier Transform ◽  
Ph Value ◽  
Chain Structure ◽  
Konjac Glucomannan ◽  
Gel Point ◽  
Wide Angle ◽  
X Ray Diffraction ◽  
X Ray ◽  
Steady State Fluorescence

Konjac glucomannan (KGM) gel was prepared by alkali catalyzed in aqueous solutions. The structure of the KGM gel was characterized by Fourier transform infrared (FTIR) spectroscopy and wide angle X-ray diffraction (WAXRD). The gel point of KGM solutions was determined by steady state fluorescence method and It was observed that the gel point of the KGM solutions depend on the concentration of KGM, pH value and temperature effectively. The results showed that the molecular chain structure of KGM gel is more regular than that of the pure KGM.

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