Search PubMed⌕ Search

Biomedical subjects

V A Bloomfield

Publications and source records attributed to V A Bloomfield.

At least 109 records · Page 6Linked to original sources
PubMed1980

Conformation of myosin in dilute solution as estimated from hydrodynamic properties.

On the basis of the current knowledge of the structure and dimensions of myosin and its parts, we analyze available data on hydrodynamic properties (translational diffusion, rotational diffusion, and intrinsic viscosity) for comparison with values calculated for models with varying geometry. Special attention is paid to detecting flexibility effects in those properties. After obtaining a plausible model for subfragment S-1, we concentrate on the conformation of the rodlike parts of myosin. Although uncertainties in the experimental values do not allow a rigorous, quantitative analysis, we show how hydrodynamic data provide evidence for the flexibility of the rod at the joint of subfragment S-2 and light meromyosin.

Chemical Phenomena↗
PubMed1980

Deglycosylated prothrombin fragment 1. Calcium binding, phospholipid interaction, and self-assocation.

The carbohydrate portion of prothrombin fragment 1 has been removed by fluorolysis in anhydrous HF. The deglycosylated protein retains its calcium- and membrane-binding properties. The slow, calcium-dependent protein transition monitored by changes in intrinsic protein fluorescence remains intact for the aglycoprotein. Calcium-dependent protein-membrane binding is also observed and can be quantitatively reversed with EDTA. The major alteration resulting from carbohydrate removal is the degree of protein self-association. Both the normal and deglycosylated proteins undergo a rapid self-association which approaches a dimer in the presence of calcium. This self-association is independent of the slow change in intrinsic fluorescence. The deglycosylated protein then undergoes a secondary self-association with kinetics identical with the fluorescence change. This secondary self-association also occurs on the membrane surface. This suggests that the calcium-dependent conformational change exposes a site on the protein which functions in secondary self-association. The carbohydrate apparently masks this site in the native molecule.

Amino Acids↗
PubMed1980

Polyelectrolyte effects in DNA condensation by polyamines.

The conditions required for the counterion induced collapse of T7 bacteriophage DNA are briefly reviewed. Using Manning's counterion condensation theory we calculate a striking unity among collapse conditions: collapse occurs when from 89% to 90% of the DNA phosphate charges are neutralized by condensed counterions. The forces involved in collapsed DNA are investigated with emphasis on electrostatic repulsion. It is concluded that polyelectrolyte repulsion is the dominant force opposing collapse. Comparison of the results or polyelectrolyte repulsion calculation made using numerical methods and the Poisson-Boltzmann equation, with values of the attractive energies due to London dispersion interactions, leads to the conclusion that dispersion forces are probably large enough to cause collapse when the repulsions have been reduced by the presence of multivalent counterions.

Calorimetry↗
PubMed1980

Comparison of polyelectrolyte theories of the binding of cations to DNA.

Predictions of the binding of counterions to DNA made using the counterion condensation theory developed by Manning are compared with those made using the Poisson-Boltzmann equation, solved numerically by the Runge-Kutta procedure. Ions are defined as territorially or atmospherically bound if they fall within a given distance, defined by counterion condensation theory, from the DNA surface. Two types of experimental situations are considered. The first is the delocalized binding of a single type of counterion to DNA. In this case the Poisson-Boltzmann treatment predicts somewhat lower extents of binding TO DNA, modeled as a 10-A radius cylinder, than does Manning theory. The two theories converge as the radius decreases. The second type of experiment is the competition of ions of different valence for binding to DNA. The theories are compared with literature values of binding constants of divalent ions in the presence of monovalent ions, and of spermidine 3+ in the presence of Na+ or Mg2+. Both predict with fair accuracy the salt dependence of the equilibrium constants.

Cations↗
PubMed1979

Counterion-induced condesation of deoxyribonucleic acid. a light-scattering study.

The addition of the trivalent or tetravalent cations spermidine or spermine to a solution of T7 DNA in aqueous solution causes an alteration of the DNA from its extended coil form to a condensed form. If performed at low DNA concentration and at low ionic strengths, this transformation results in a monomolecular collapse to form a particle with a hydrodynamic radius of about 500 A. We have monitored this change using quasielastic and total intensity light scattering. In a solution of 50% methanol in water, the divalent cations Mg2+ and putrescine also can cause the condensation of DNA. Using Manning's (1978) counterion condensation theory, we calculate a striking unity among these disparate ions: the collapse occurs in each case when from 89 to 90% of the DNA phosphate charges are neutralized by condensed counterions.

Chemical Phenomena↗
PubMed1979

Determination of polymer size distribution by combination of quasielastic light scattering and band transport: evaluation of the effect of diffusion.

In this paper we report a computer simulation study of the effect of diffusion on the size distribution obtained by combining light scattering with isokinetic band sedimentation or electrophoresis. We find that, under typical experimental conditions, the method yields reasonably accurate size distributions for samples of particles greater than 10 nm radius. However, caution should be exercised in interpreting the results for smaller particles, for which the distortion due to diffusion can be considerable.

Journal Article↗
PubMed1979

Diffusion-controlled reactions on spherical surfaces. Application to bacteriophage tail fiber attachment.

We have explored the kinetic implications of a model that may account for the acceleration of tail fiber (F) attachment to baseplates (B) by whiskers (W) on bacteriophage T4. The model assumes that a W-F complex is formed initially, and that the tethered fiber then undergoes rotational diffusion until a B-F encounter takes place. In the absence of whiskers, B-F complexes must form unassisted. Formation of a W-F intermediate will accelerate F attachment to B if (a) the bimolecular rate constant for W-F complex formation is larger than that for direct B-F interaction and (b) subsequent rotational diffusion of the tip of F to B is not much slower than the dissociation of W-F. Condition a was investigated by applying a recent theory of orientational effects on translational diffusion-controlled reactions. This theory suggests that substantial rate enhancement is expected if the reaction half-angle theta 0 is larger for W-F than for B-F complex formation. Condition b was investigated by calculating the mean and the variance of the time required for the diffusion of a molecule (the proximal tip of the fiber) on a spherical surface (whose radius is the distance from the tip to the whisker tethering point) into a circular sink (the baseplate site). The mean time is on the order of the inverse rotational diffusion coefficient, DR, of the fiber, but is sensitive to theta 0. Both conditions are satisfied for plausible choices of parameters. The solution to the diffusion equation we have obtained should have application to other physical situations, such as the rate of quenching of a fluorophore as it diffuses on the surface of a spherical membrane into proximity with a quencher.

Diffusion↗
PubMed1979

Association of proteins.

A review is presented of the various intermolecular forces important in stabilizing protein structure and association. Emphasis is put on entropic as well as enthalpic contributions to the free energy. The factors affecting size and size distribution in protein aggregates are discussed. A theory is presented for the size distribution of casein micelles, taking into account the spherical nature of the micelles and the importance of surface repulsive forces in limiting size.

Caseins↗