Photon-Count Autocorrelation Spectroscopy. Data Analysis in the Case of Monoexponential Spectra

Nieuwenhuysen, Paul

doi:10.1021/ma60064a040

Cited by 17 publications

(11 citation statements)

References 1 publication

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“…Cumulant Analysis. As a first analysis, the cumulant method proposed by Koppel (Koppel, 1972;Nieuwenhuysen, 1978) was used. In this method, no hypothesis is made about the distribution of F = DK2.…”

Section: Photon Correlation Spectroscopymentioning

confidence: 99%

“…For a volume fraction 0 < 0.035 the normalized second-order cumulant, the Q factor, is <0.10 for our aL-crystallin solutions. The deviation from 0 can be attributed to perturbations by dust particles and, therefore, P was obtained by an extrapolation to Q = 0 (Nieuwenhuysen, 1978). But from 4 > 0.035 on, a distinct and gradual increase in the Q value is observed and the correlation function shows a slowly decaying component.…”

Section: Photon Correlation Spectroscopymentioning

confidence: 99%

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Photon correlation spectroscopy and light scattering of eye lens proteins at high concentrations

Andries¹,

Clauwaert²

1985

Biophysical Journal

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The bovine eye lens protein, alpha L crystallin, has been studied with photon correlation spectroscopy and statical light scattering in the concentration range up to 200 g/l in different solvent conditions. At higher concentration (c greater than 70 g/l) the scattering behavior is quite complicated, which results in nonexponential correlation functions. Three methods have been used for the analysis of these correlation functions, namely, cumulant analysis, sum of two exponentials analysis, and exponential sampling method. These methods resulted in very similar results. The highly concentrated solutions contain two scattering entities: the single alpha L crystallin and a rather heterogeneous population of large clusters. The statical light-scattering experiments can be interpreted in the same way and gave consistent results for the dimensions of the large scattering units. The formation of these clusters, which are strong light scatterers, is superimposed on an increasing degree of correlation between the bulk of the alpha L-crystallins, resulting in a net decrease of light scattering as a function of concentration.

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Section: Photon Correlation Spectroscopymentioning

confidence: 99%

Section: Photon Correlation Spectroscopymentioning

confidence: 99%

Photon correlation spectroscopy and light scattering of eye lens proteins at high concentrations

Andries¹,

Clauwaert²

1985

Biophysical Journal

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“…In the case of a dilute and monodisperse solution of macromolecules, which are small compared with the wavelength of the light, the measured correlation function G(iT) decays exponentially with a decay time proportional to the desired diffusion coefficient D: G(iT) = A + B * exp (-2 D K2.iT) where i is the channel number, T is the chosen sample time, K is the known modulus of the scattering vector and A and B are constants. We have previously described our set-up and experimental procedures (Nieuwenhuysen & Clauwaert, 1977, 1978 and methods of data analysis (Nieuwenhuysen, 1978).…”

Section: Photon Correlation Spectroscopy Ofscattered Lightmentioning

confidence: 99%

“…unfavourable measurement conditions, caused by the limited solubility so that the maximum concentration was 6 mg/ml for both proteins, the quality factor Q of individual spectra ranged from -0.1 to 0.2. The numerous spectra were all taken into account to allow an optimal estimate of the diffusion coefficients as described previously (Nieuwenhuysen, 1978). No concentration-dependence was found.…”

Section: Sedimentation Coefficientmentioning

confidence: 99%

Pro-(carboxypeptidases A) from whole pig pancreas. Their mass, size, shape and solvation

Martínez¹,

Nieuwenhuysen²,

Clauwaert³

et al. 1983

Biochemical Journal

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Sedimentation analysis and light-scattering measurements were made with the two forms of pig pancreas pro-(carboxypeptidase A), in order to determine some of their physical properties. The following values were found (the first value applies to the binary complex and the second one to the monomer). The A 1%/280.1 cm values were 19.9 +/- 0.3 and 16.3 +/- 0.3. The partial specific volumes v -0 were 0.707 +/- 0.016 cm3/g and 0.714 +/- 0.015 cm3/g. The sedimentation coefficients S 0/20,w were 4.90 +/- 0.15S and 3.75 +/- 0.15 S. The diffusion coefficients D 0/20,w were (5.8 +/- 0.1) X 10(-7) cm2/s and (6.95 +/- 0.15) X 10(-7) cm2/s. From these data the following values were calculated. Relative molecular masses Mr were 71 000 +/- 4000 and 46 000 +/- 3000. The frictional ratios f/fmin. were 1.37 +/- 0.06 and 1.31 +/- 0.07; assuming a value for the solvation of the molecules (delta = 0.5 g/g) the asymmetry values range from 3 to 5 for the binary complex and from 2 to 4 for the monomer. The Mr values found in the present work coincide with those found by means of polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate [Martínez, Avilés, SanSegundo & Cuchillo (1981) Biochem. J. 197, 141-147]. Therefore the low values obtained by those authors when using gel-filtration chromatography must be the result of the interaction of the zymogens with the gel matrix, as the asymmetry is too small to justify the large discrepancies found.

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“…The translational diffusion coefficient, D, of the rRNA in Brownian motion was determined by analysing the intensity fluctuations of their laser light scattering, by using single-clipped photoncount autocorrelation spectroscopy (see, e.g., Koppel, 1974;Nieuwenhuysen, 1978;Nieuwenhuysen & Clauwaert, 1978). The measured correlation function decays exponentially with a decay time proportional to D: G(iT) = A + B exp where i is the channel number, T the chosen sample time, and K the known modulus of the scattering vector; A and B are constants.…”

Section: Photon Correlation Spectroscopy Of Scattered Laser Lightmentioning

confidence: 99%

The size and conformation of Artemia (brine-shrimp) ribosomal RNA free in solution

Donceel¹,

Nieuwenhuysen²,

Clauwaert³

1982

Biochemical Journal

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The RNA was isolated from the large ribosomal subunits of the brine shrimp Artemia, and its conformation free in solution was studied by determining its sedimentation and diffusion coefficients. A comparison was made of the hydrodynamic radius of the ribosomal subunit and its isolated RNA in various buffers. The conformation of the rRNA free in solution is more extended than when it is incorporated in the ribosome. This is not only the case when the rRNA solution lacks bivalent and polyvalent cations, but even in the presence of Mg2+ and spermidine, which cause a tightening of RNA. Thus the ribosomal proteins should induce a further tightening of the rRNA during the assembly of the ribosome. In the discussion, the reported data on Escherichia coli rRNA species are presented in such a way that large discrepancies between various studied are revealed, and that they can be compared with the data reported here on the larger rRNA of an eukaryote.

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Photon-Count Autocorrelation Spectroscopy. Data Analysis in the Case of Monoexponential Spectra

Cited by 17 publications

References 1 publication

Photon correlation spectroscopy and light scattering of eye lens proteins at high concentrations

Photon correlation spectroscopy and light scattering of eye lens proteins at high concentrations

Pro-(carboxypeptidases A) from whole pig pancreas. Their mass, size, shape and solvation

The size and conformation of Artemia (brine-shrimp) ribosomal RNA free in solution

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