Molecular Structure of Elastomers Determined with Carbon-13 NMR

1975 ◽  
Vol 48 (4) ◽  
pp. 705-718 ◽  
Author(s):  
C. J. Carman ◽  
K. C. Baranwal

Abstract Characterization and identification of elastomers are important analytical needs for those involved in rubber technology. High resolution pulsed Fourier transform 13C NMR has been shown to be a powerful tool which can supply much detail as to sequence distribution, chain configuration, steric purity, or identification of polymer mixtures. One can also use 13C to distinguish polymer blends from copolymers of similar composition. This information about elastomers commonly used in the rubber industry provides not only a new tool for analytical problem solving, but also provides analytical information to guide the chemist as he makes elastomeric materials with structural features which impart specific physical properties.

1993 ◽  
Vol 115 (23) ◽  
pp. 10845-10848 ◽  
Author(s):  
G. Knuchel ◽  
G. Grassi ◽  
B. Vogelsanger ◽  
A. Bauder

1989 ◽  
Vol 43 (8) ◽  
pp. 1387-1393 ◽  
Author(s):  
William F. McDonald ◽  
Hans Goeitler ◽  
Marek W. Urban

A new rheo-photoacoustic Fourier transform infrared cell has been developed to perform stress-strain studies on polymeric materials. The rheo-photoacoustic measurements lead to the enhancement of the photoacoustic signal and allow one to monitor the effect of elongational forces on the molecular structure of polymers. Propagating acoustic waves are detected as a result of the deformational changes and thermal property changes upon the applied stress. Applications of this technique to fibers, films, and adhesion of thin films are presented.


1990 ◽  
Vol 68 (11) ◽  
pp. 1482-1488 ◽  
Author(s):  
Balwant S. Tuana ◽  
Brian J. Murphy

The development of specific pharmacological agents that modulate different types of ion channels has prompted an extensive effort to elucidate the molecular structure of these important molecules. The calcium channel blockers that specifically modulate the L-type calcium channel activity have aided in the purification and reconstitution of this channel from skeletal muscle transverse tubules. The L-type calcium channel from skeletal muscle is composed of five subunits designated α1, α2, β, γ, and σ. The α1-subunit is the pore-forming polypeptide and contains the ligand binding and phosphorylation sites through which channel activity can be modulated. The role of the other subunits in channel function remains to be studied. The calcium channel components have also been partially purified from cardiac muscle. The channel consists of at least three subunits that have properties related to the subunits of the calcium channel from skeletal muscle. A core polypeptide that can form a channel and contains ligand binding and phosphorylation sites has been identified in cardiac preparations. Here we summarize recent biochemical and molecular studies describing the structural features of these important ion channels.Key words: dihydropyridine receptor, calcium channel, muscle, molecular structure.


2009 ◽  
Vol 131 (20) ◽  
pp. 204301 ◽  
Author(s):  
Helen O. Leung ◽  
Mark D. Marshall ◽  
Tasha L. Drake ◽  
Tadeuz Pudlik ◽  
Nazir Savji ◽  
...  

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