Protein–Polymer Interaction Characteristics Unique to Nanoscale Interfaces: A Perspective on Recent Insights

Author(s):  
David H. Cho ◽  
Jong-in Hahm
2014 ◽  
Vol 21 (2) ◽  
Author(s):  
Florian Capito ◽  
Harald Kolmar ◽  
Bernd Stanislawski ◽  
Romas Skudas

1981 ◽  
Author(s):  
R. M. Gendreau ◽  
S. Winters ◽  
L. Lee ◽  
R. I. Leininger ◽  
R. J. Jakobsen

BioResources ◽  
2007 ◽  
Vol 2 (1) ◽  
pp. 20-33
Author(s):  
Jung Myoung Lee ◽  
John A. Heitmann ◽  
Joel J. Pawlak

The effect of cellulase treatments on the rheology of carboxymethyl cellulose (CMC) solutions was studied using a rotational viscometer. The rheological behaviors of CMC solutions of different molecular mass and degrees of substitution where studied as a function of time after various treatments. These solutions were subjected to active and heat-denatured cellulase, a cationic polyelectrolyte (C-PAM), as well as different shear rates. A complex protein-polymer interaction was observed, leading to a potential error source in the measurement of enzymatic activity by changes in the intrinsic viscosity. The interaction was termed a polymeric effect and defined as a reduction in viscosity of the substrate solution without significant formation of reducing sugars from enzymatic hydrolysis. The cause of the reduction in viscosity appears to be related to the interaction between the enzymes as amphipathic particles and the soluble CMC. Thus, the polymeric effect may cause a considerable experimental error in the measurement of enzymatic activity by viscometric methods.


Author(s):  
G. C. Ruben ◽  
K. Iqbal ◽  
I. Grundke-Iqbal ◽  
H. Wisniewski ◽  
T. L. Ciardelli ◽  
...  

In neurons, the microtubule associated protein, tau, is found in the axons. Tau stabilizes the microtubules required for neurotransmitter transport to the axonal terminal. Since tau has been found in both Alzheimer neurofibrillary tangles (NFT) and in paired helical filaments (PHF), the study of tau's normal structure had to preceed TEM studies of NFT and PHF. The structure of tau was first studied by ultracentrifugation. This work suggested that it was a rod shaped molecule with an axial ratio of 20:1. More recently, paraciystals of phosphorylated and nonphosphoiylated tau have been reported. Phosphorylated tau was 90-95 nm in length and 3-6 nm in diameter where as nonphosphorylated tau was 69-75 nm in length. A shorter length of 30 nm was reported for undamaged tau indicating that it is an extremely flexible molecule. Tau was also studied in relation to microtubules, and its length was found to be 56.1±14.1 nm.


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