Light-scattering study of the oxidative degradation of polystyrene

1964 ◽  
Vol 2 (3) ◽  
pp. 1205-1220 ◽  
Author(s):  
James C. Spitsbergen ◽  
Harold C. Beachell
Keyword(s):  
Light Scattering ◽  
Oxidative Degradation ◽  
Scattering Study

Phase transitions in C2O4HNH4, 1/2 H2O. A light scattering study at normal pressure

1987 ◽  
Vol 48 (5) ◽  
pp. 809-819 ◽  
Author(s):  
J.L. Godet ◽  
M. Krauzman ◽  
J.P. Mathieu ◽  
H. Poulet ◽  
N. Toupry
Keyword(s):  
Phase Transitions ◽  
Light Scattering ◽  
Normal Pressure ◽  
Scattering Study

scholarly journals Assembly of fibrin. A light scattering study.

1979 ◽  
Vol 254 (22) ◽  
pp. 11272-11281
Author(s):  
R.R. Hantgan ◽  
J. Hermans
Keyword(s):  
Light Scattering ◽  
Scattering Study

Dynamic-light-scattering study of the solid-liquid interface in succinonitrile during growth

1990 ◽  
Vol 41 (2) ◽  
pp. 1142-1144 ◽  
Author(s):  
J-M. Laherrère ◽  
H. Savary ◽  
R. Mellet ◽  
J-C. Tolédano
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Liquid Interface ◽  
Scattering Study ◽  
Solid Liquid Interface ◽  
Solid Liquid

scholarly journals Lateral association and elongation of vimentin intermediate filament proteins: A time-resolved light-scattering study

2016 ◽  
Vol 113 (40) ◽  
pp. 11152-11157 ◽  
Author(s):  
Carlos G. Lopez ◽  
Oliva Saldanha ◽  
Klaus Huber ◽  
Sarah Köster
Keyword(s):  
Light Scattering ◽  
Quantitative Model ◽  
Radius Of Gyration ◽  
Time Resolved ◽  
Intermediate Filament Proteins ◽  
Hierarchical Assembly ◽  
Lateral Association ◽  
Cytoskeletal Filament ◽  
Longitudinal Association ◽  
Scattering Study

Vimentin intermediate filaments (IFs) are part of a family of proteins that constitute one of the three filament systems in the cytoskeleton, a major contributor to cell mechanics. One property that distinguishes IFs from the other cytoskeletal filament types, actin filaments and microtubules, is their highly hierarchical assembly pathway, where a lateral association step is followed by elongation. Here we present an innovative technique to follow the elongation reaction in solution and in situ by time-resolved static and dynamic light scattering, thereby precisely capturing the relevant time and length scales of seconds to minutes and 60–600 nm, respectively. We apply a quantitative model to our data and succeed in consistently describing the entire set of data, including particle mass, radius of gyration, and hydrodynamic radius during longitudinal association.

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