S
Sow-Hsin Chen
Researcher at Massachusetts Institute of Technology
Publications - 294
Citations - 14458
Sow-Hsin Chen is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Neutron scattering & Small-angle neutron scattering. The author has an hindex of 61, co-authored 294 publications receiving 13793 citations. Previous affiliations of Sow-Hsin Chen include Centre national de la recherche scientifique & University of Messina.
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Journal ArticleDOI
Analysis of small angle neutron scattering spectra from polydisperse interacting colloids
Michael Kotlarchyk,Sow-Hsin Chen +1 more
TL;DR: In this paper, a simple procedure for analyzing small angle neutron scattering (SANS) spectra from interacting colloids containing a continuous distribution of particle sizes is presented. But the applicability of the procedure to the analysis of real data is demonstrated with spectra taken from water-in-oil microemulsions, ionic micelles, and interacting proteins.
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Experimental determination of the nature of diffusive motions of water molecules at low temperatures.
TL;DR: Extensive and high-quality quasi-elastic incoherent neutron scattering data were obtained for water in the temperature range extending from room temperature down to —20 C in the supercooled state, and two relaxation times are clearly identified which are related to the short-time and intermediate-time diffusion of water molecules.
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Pressure Dependence of Fragile-to-Strong Transition and a Possible Second Critical Point in Supercooled Confined Water
TL;DR: It is shown that the transition temperature decreases steadily with an increasing pressure, until it intersects the homogenous nucleation temperature line of bulk water at a pressure of 1600 bar, and above this pressure it is no longer possible to discern the characteristic feature of the FS transition.
Journal ArticleDOI
Small Angle Neutron Scattering Studies of the Structure and Interaction in Micellar and Microemulsion Systems
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Observation of fragile-to-strong dynamic crossover in protein hydration water.
TL;DR: It is demonstrated experimentally that this sudden switch in dynamic behavior of the hydration water on lysozyme occurs precisely at 220 K and can be described as a fragile-to-strong dynamic crossover.