Small-Angle Neutron Scattering as a Probe for Protein Aggregation at Many Length Scales

2006 ◽  
pp. 125-146 ◽  
Author(s):  
Susan Krueger ◽  
Derek Ho ◽  
Amos Tsai
1989 ◽  
Vol 166 ◽  
Author(s):  
P. Wiltzius ◽  
S. B. Dierker

ABSTRACTWe present small angle neutron scattering data of porous glasses. Analysis of the structure factor shows that the morphology on length scales between 30 A and 800 A depends on fabrication procedures. Fast gelation leads to a clumpy glass, whereas slow gelation produces a random smooth internal interface.


1994 ◽  
Vol 376 ◽  
Author(s):  
Rex P. Hjelm ◽  
Wesley Wampler ◽  
Michel Gerspacher

ABSTRACTAs part of our work on the structure of composite materials we have been exploring the use of small-angle neutron scattering using the method of contrast variation to dissect the component form, structure and distribution. This approach has resulted in a new look at very old problemreinforcement of elastomers by carbon black.Using this approach we studied an experimental high surface area (HSA) carbon black and a gel of "HSA-bound" rubber in cyclohexane/deuterocyclohexane mixtures. HSA in cyclohexane is found to be short rodlike particle aggregates. The aggregates have a shell-core structure with a high density graphitic outer shell and an inner core of lower density amorphous carbon. The core is continuous throughout the carbon black aggregate, making the aggregate a stiff, integral unit. Contrast variation of swollen composite gels shows that there are two length scales in the gel structure. Above 10 Å, scattering from carbon black predominates, and below 10 Å the scattering is from both carbon black and the elastomer. The HSA in the composite is completely embedded in polyisoprene. An estimate of the carbon black structure factor shows strong exclusion of neighboring aggregates, probably from excluded volume effects. The surface structure of the carbon black is unaltered by the interactions with elastomer and appears smooth over length scales above about 10 Å. These results show that contrast variation can provide information on composite structure that is not available by other means. This information relates to the reinforcement mechanism of elastomers by carbon blacks.


1999 ◽  
Vol 32 (9) ◽  
pp. 3093-3096 ◽  
Author(s):  
M. Agamalian ◽  
R. G. Alamo ◽  
M. H. Kim ◽  
J. D. Londono ◽  
L. Mandelkern ◽  
...  

2009 ◽  
Vol 11 (6) ◽  
pp. 441-445 ◽  
Author(s):  
Melissa A. Sharp ◽  
P. Klaus Pranzas ◽  
Andreas Schreyer

2004 ◽  
Vol 201 (15) ◽  
pp. 3354-3360 ◽  
Author(s):  
A. Grob ◽  
S. Saranu ◽  
U. Herr ◽  
A. Michels ◽  
R. N. Viswanath ◽  
...  

2018 ◽  
Author(s):  
James I Austerberry ◽  
Daniel J Belton

AbstractThe rapid and complex nature of protein aggregation makes the identification of aggregation mechanisms and their precursors challenging. Here we demonstrate the novel use of small-angle neutron scattering to perform dynamic real-time measurement and analysis of protein aggregation. Changes in bovine serum albumin monomer population and aggregate size are identified at several isothermal temperatures. Kratky plots indicate that the aggregation of BSA occurs through the partial unfolding of the monomer. Dual population modelling of the scattering data indicates that the protein nucleates and grows through a two stage mechanism; a rapid burst phase and a slower growth phase. Both stages are observed to follow Arrhenius behaviour between 70-80 °C.


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