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Maria Monica Castellanos

Researcher at National Institute of Standards and Technology

Publications -  11
Citations -  295

Maria Monica Castellanos is an academic researcher from National Institute of Standards and Technology. The author has contributed to research in topics: Neutron scattering & Small-angle scattering. The author has an hindex of 8, co-authored 9 publications receiving 241 citations. Previous affiliations of Maria Monica Castellanos include Pennsylvania State University.

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Both protein adsorption and aggregation contribute to shear yielding and viscosity increase in protein solutions

TL;DR: Evidence of a bulk yield stress arising from protein aggregation is presented, and correlated with results from standard characterization techniques used in the bio-pharmaceutical industry.
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Molecular dynamics simulations of human serum albumin and role of disulfide bonds.

TL;DR: Removing all disulfide bonds in the protein appears to be a practical prescreening tool for identifying disulfides relevant to structure and dynamics, and could have similar consequences in other proteins of interest, such as immunoglobulin G.
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Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering.

TL;DR: The use of small-angle neutron scattering is described to study the solution structure of biological molecules and the packing arrangement in amorphous phases, that is, frozen glasses and freeze-dried protein powders.
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Explaining the non-newtonian character of aggregating monoclonal antibody solutions using small-angle neutron scattering.

TL;DR: Fractal submicrometer particles are demonstrated to be responsible for the increase in low shear rate viscosity and low wavevector upturn in scattered intensity of aggregated antibody solutions; both are removed from aggregated samples by filtering.
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Role of Molecular Flexibility and Colloidal Descriptions of Proteins in Crowded Environments from Small-Angle Scattering.

TL;DR: This study investigates the role of multiple protein configurations in the interaction parameters derived from small-angle scattering for proteins in concentrated solutions and provides insights to determine the length scales where isotropic colloidal models can be used, and find smoothly varying sets of interaction parameters that encompass ensembles of structures.