Molecular Weight Dependence of Shear Viscosity of a Polymer Monolayer:  Evidence for the Lack of Chain Entanglement in the Two-Dimensional Plane

1998 ◽  
Vol 31 (8) ◽  
pp. 2673-2675 ◽  
Author(s):  
Nobuhiro Sato ◽  
Shinzaburo Ito ◽  
Masahide Yamamoto
1959 ◽  
Vol 32 (1) ◽  
pp. 48-66 ◽  
Author(s):  
W. G. Forbes ◽  
L. A. McLeod

Abstract A method has been developed for the measurement of the tack strength of fresh and reproducibly smooth rubber surfaces. Using this method the tack strength of natural rubber is shown to be independent of polymer purity, and, to a large extent, Mooney viscosity, intrinsic viscosity, gel content and molecular weight distribution. The relative tack strengths of polyisoprenes of different molecular weights prepared in different catalyst systems are measured. The results are discussed in terms of microstructure. A study of the tack strength of oil-extended butadiene-styrene copolymers indicates that relative tack strength is related to the shear viscosity of the bulk polymer. Measurements of relative tack strength on Alfin and free radical butadiene-styrene copolymers, butyl, brominated butyl and butadiene-acrylonitrile copolymers confirm the inportance of shear viscosity in controlling tack strength. Choice of catalyst system and temperature of polymerization cause the largest variation in polymer viscosity. The contact time required for the relative tack strength to become unity is shown to be inversely dependent upon the value of the relative tack strength itself. Shear viscosity measurements are given for six classes of polymer and the values shown to correlate with relative tack strength. It is postulated that molecular weight (and probably also chain entanglement) is the controlling variable. The bond strength between two different uncured polymers is shown to depend upon the difference in cohesive energy densities of the two polymers.


Author(s):  
H.A. Cohen ◽  
W. Chiu ◽  
J. Hosoda

GP 32 (molecular weight 35000) is a T4 bacteriophage protein that destabilizes the DNA helix. The fragment GP32*I (77% of the total weight), which destabilizes helices better than does the parent molecule, crystallizes as platelets thin enough for electron diffraction and electron imaging. In this paper we discuss the structure of this protein as revealed in images reconstructed from stained and unstained crystals.Crystals were prepared as previously described. Crystals for electron microscopy were pelleted from the buffer suspension, washed in distilled water, and resuspended in 1% glucose. Two lambda droplets were placed on grids over freshly evaporated carbon, allowed to sit for five minutes, and then were drained. Stained crystals were prepared the same way, except that prior to draining the droplet, two lambda of aqueous 1% uranyl acetate solution were applied for 20 seconds. Micrographs were produced using less than 2 e/Å2 for unstained crystals or less than 8 e/Å2 for stained crystals.


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