Translational Diffusion Constants and Intermolecular Relaxation in Paramagnetic Solutions with Hyperfine Coupling on the Electronic Site

1998 ◽  
Vol 102 (21) ◽  
pp. 3674-3680 ◽  
Author(s):  
E. Belorizky ◽  
D. G. Gillies ◽  
W. Gorecki ◽  
K. Lang ◽  
F. Noack ◽  
...  
1977 ◽  
Author(s):  
E. Serrallach ◽  
W. Känzig ◽  
V. Hofmann ◽  
P.W. Straub ◽  
M. Zulauf

The intriguing diversity of published translational diffusion constants for the fibrinogen molecule can hardly be explained, unless interactions between the molecules are postulated. In the present study we have investigated the possible effect of molecular association and electrostatic intermolecular interactions on the Brownian motion. The translational diffusion coefficient DT, the rotational diffusion coefficient around the minor axis DR and the sedimentation coefficient have been measured. The methods used were dynamic light scattering and analytical ultracentrifugation. The samples were solutions of purified human fibrinogen. The correlation-function corresponding to DT deviates from a single exponential. The initial slope is found to depend on concentration, being DT = (1.7 ± 0.3) 10-7 cm2/s at 10mg/ml, pH 7.4 and 0.15 molar Tris-NaCl, and increases at fibrinogen concentrations below 2mg/ml. These results are compatible with a polydispers solution, in which single molecules are in equilibrium with pair and higher aggregates. The nature of the aggregates is end-to-end as indicated from the difference between the two rotational diffusion constants DR = 40000 ± 20% and DR = 10000 ±30% s-1. On the basis of the Hall-Slayter model and assumption of end-to-end association we calculated the ratio of the sedimentation coefficient of single, pair and triplet associates, being 1:1.14:1.20. Therefore, it is difficult to separate them in a sedimentation run. For ionic strength below 0.05 molar and low fibrinogen concentration (0.lmg/ml) a fast decay appears in the correlation, indicating that the Brownian motion is strongly influenced by electrostatic interactions.


1995 ◽  
Vol 33 (13) ◽  
pp. S107-S113 ◽  
Author(s):  
Susan A. Fawthrop ◽  
Duncan G. Gillies ◽  
Leslie H. Sutcliffe ◽  
Mark R. Symms

1995 ◽  
Vol 91 (5) ◽  
pp. 887 ◽  
Author(s):  
Caroline A. Beadle ◽  
Duncan G. Gillies ◽  
Leslie H. Sutcliffe ◽  
Xiaoping Wu

Author(s):  
E. Keyhani

The matrix of biological membranes consists of a lipid bilayer into which proteins or protein aggregates are intercalated. Freeze-fracture techni- ques permit these proteins, perhaps in association with lipids, to be visualized in the hydrophobic regions of the membrane. Thus, numerous intramembrane particles (IMP) have been found on the fracture faces of membranes from a wide variety of cells (1-3). A recognized property of IMP is their tendency to form aggregates in response to changes in experi- mental conditions (4,5), perhaps as a result of translational diffusion through the viscous plane of the membrane. The purpose of this communica- tion is to describe the distribution and size of IMP in the plasma membrane of yeast (Candida utilis).Yeast cells (ATCC 8205) were grown in synthetic medium (6), and then harvested after 16 hours of culture, and washed twice in distilled water. Cell pellets were suspended in growth medium supplemented with 30% glycerol and incubated for 30 minutes at 0°C, centrifuged, and prepared for freeze-fracture, as described earlier (2,3).


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