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S Sedimentation coefficient

D=mass diffumsion coefficient Z)T=fiiermal diffusion coefficient /=friction coefficient G=(oh (centrifugal acceleration) / =Boltzniann constant meff=particle effective mass r=radius of centrifuge basket s=sedimentation coefficient T = absolute temperature =geometric volume of die channel w=channel thickness y=diermal expansion coefficient p=electrophoretic... [Pg.336]

D diffusion coefficient hr> distance from the center of rotation s sedimentation coefficient CO angtdar velocity... [Pg.10]

Sedimentation coefficient determined from migration of gradient curve median s, Sedimentation coefficient determined from... [Pg.1566]

The stationary-state velocity per unit acceleration is a parameter which characterizes the settling particle and is called the sedimentation coefficient s ... [Pg.636]

The particle can be assumed to be spherical, in which case M/N can be replaced by (4/3)ttR P2, and f by 671770R- In this case the radius can be evaluated from the sedimentation coefficient s = 2R (p2 - p)/9t7o. Then, working in reverse, we can evaluate M and f from R. These quantities are called, respectively, the mass, friction factor, and radius of an equivalent sphere, a hypothetical spherical particle which settles at the same rate as the actual molecule. [Pg.638]

Fig. 2. Ultracentrifugal pattern for the water-extractable proteins of defatted soybean meal in pH 7.6, 0.5 ionic strength buffer. Numbers above peaks are approximate sedimentation coefficients in Svedberg units, S. Molecular weight ranges for the fractions are 2S, 8,000—50,000 7S, 100,000—180,000 IIS, 300,000—350,000 and 15S, 600,000—700,000 (9). The 15S fraction is a dimer of the IIS protein (10). Fig. 2. Ultracentrifugal pattern for the water-extractable proteins of defatted soybean meal in pH 7.6, 0.5 ionic strength buffer. Numbers above peaks are approximate sedimentation coefficients in Svedberg units, S. Molecular weight ranges for the fractions are 2S, 8,000—50,000 7S, 100,000—180,000 IIS, 300,000—350,000 and 15S, 600,000—700,000 (9). The 15S fraction is a dimer of the IIS protein (10).
Centrifugation methods separate macromolecules on the basis of their characteristic densities. Particles tend to fail through a solution if the density of the solution is less than the density of the particle. The velocity of the particle through the medium is proportional to the difference in density between the particle and the solution. The tendency of any particle to move through a solution under centrifugal force is given by the sedimentation coefficient, S ... [Pg.157]

Sedimentation coefficients are a measure of the velocity witli which a particle sediments in a centrifugal force field. Sedimentation coefficients are typically expressed in Svedbergs (.symbolized S), named to honor The Svedberg, developer of the ultracentrifuge. One S equals 10 . sec. [Pg.343]

Ribosomes are ancient ribonucleoprotein complexes that are the sites of protein synthesis in living cells. Their core structures and fundamental functional mechanisms have been conserved throughout the three domains of life bacteria, archaea and eukaryotes. All ribosomes are organized into two subunits that are defined by their apparent sedimentation coefficient, measured in Svedberg units (S). There is a general... [Pg.1085]

Analytical ultracentrifugation (AUC) Molecular weight M, molecular weight distribution, g(M) vs. M, polydispersity, sedimentation coefficient, s, and distribution, g(s) vs. s solution conformation and flexibility. Interaction complex formation phenomena. Molecular charge No columns or membranes required [2]... [Pg.213]

Traditional analysis methods on these measurements have been based around recording the movement of the radial position of the boundary r y with time t, from which a sedimentation coefficient, 5 (sec or Svedbergs, S, where 1 S = 10 sec) can be obtained (see, e.g. [30]) ... [Pg.219]

Fig. 3 Concentration dependence of the sedimentation coefficient for wheat amylopectin. The data have been fitted to Eq. 5 (see text) yielding s = (120d= 10)S, = (170=b60)ml/g... Fig. 3 Concentration dependence of the sedimentation coefficient for wheat amylopectin. The data have been fitted to Eq. 5 (see text) yielding s = (120d= 10)S, = (170=b60)ml/g...
The simplest way computationally of obtaining a sedimentation coefficient distribution is from time derivative analysis of the evolving concentration distribution profile across the cell [40,41]. The time derivative at each radial position r is d c r,t)/co /dt)r where cq is the initial loading concentration. Assuming that a sufficiently small time integral of scans are chosen so that Ac r t)/At= dc r t)ldt the apparent weight fraction distribution function g (s) n.b. sometimes written as (s ) can be calculated... [Pg.221]

In this relation a(r, t) is the experimentally observed signal, s represents random noise, axi r) represents the time invariant systematic noise and aRi(f) the radial invariant systematic noise Schuck [42] and Dam and Schuck [43] describe how this systematic noise is ehminated. x is the normahsed concentration at r and t for a given sedimenting species of sedimentation coefficient 5 and translational diffusion coefficient D it is normalised to the initial loading concentration so it is dimensionless. [Pg.223]

Although only approximate analytical solutions to this partial differential equation have been available for x(s,D,r,t), accurate numerical solutions are now possible using finite element methods first introduced by Claverie and coworkers [46] and recently generalized to permit greater efficiency and stabihty [42,43] the algorithm SEDFIT [47] employs this procedure for obtaining the sedimentation coefficient distribution. [Pg.223]

The sedimentation coefficient s°, or its normalized form 5 0 w function of the conformation and flexibility of a macromolecule (via its translational frictional property) and its mass. So if we are going to obtain conformation and flexibility information we need to know the molecular weight (molar mass)... [Pg.225]

A sedimentation coefficient distribution—either c s) versus 5 or g (s) vs. s—for a polysaccharide can also be converted into an apparent molecular weight distribution if the conformation of the polysaccharide is known or can... [Pg.226]

One can see the M procedure has a parallel to either g (s) vs. s or c(s) vs. s in sedimentation velocity where the data are transformed from radial displacement space [concentration, c(r) versus r] to sedimentation coefficient space [g s) or c(s) versus s]. Here we are transforming the data from concentration space [concentration relative to the meniscus j(r) versus r] to molecular weight space [M r) versus r]. [Pg.230]

The sedimentation coefficient for wormlike chains was first worked out by Hearst and Stockmayer [123], later improved by Yamakawa and Fujii [124] to give this expression for s ... [Pg.241]


See other pages where S Sedimentation coefficient is mentioned: [Pg.201]    [Pg.107]    [Pg.14]    [Pg.448]    [Pg.32]    [Pg.339]    [Pg.216]    [Pg.459]    [Pg.118]    [Pg.186]    [Pg.39]    [Pg.186]    [Pg.229]    [Pg.257]    [Pg.278]    [Pg.278]    [Pg.1296]    [Pg.388]    [Pg.208]    [Pg.28]    [Pg.201]    [Pg.107]    [Pg.14]    [Pg.448]    [Pg.32]    [Pg.339]    [Pg.216]    [Pg.459]    [Pg.118]    [Pg.186]    [Pg.39]    [Pg.186]    [Pg.229]    [Pg.257]    [Pg.278]    [Pg.278]    [Pg.1296]    [Pg.388]    [Pg.208]    [Pg.28]    [Pg.84]    [Pg.106]    [Pg.636]    [Pg.638]    [Pg.238]    [Pg.221]    [Pg.223]    [Pg.224]    [Pg.225]    [Pg.243]   
See also in sourсe #XX -- [ Pg.9 , Pg.16 ]




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