scispace - formally typeset
P

Prasad Sarangapani

Researcher at Regeneron

Publications -  18
Citations -  591

Prasad Sarangapani is an academic researcher from Regeneron. The author has contributed to research in topics: Globular protein & Length scale. The author has an hindex of 11, co-authored 17 publications receiving 501 citations. Previous affiliations of Prasad Sarangapani include MedImmune & University of Notre Dame.

Papers
More filters
Journal ArticleDOI

Protein aggregation, particle formation, characterization & rheology

TL;DR: This review attempts to give a concise overview of recent progress made in mechanistic understanding of protein aggregation, particulate formation and protein solution rheology and highlights some areas of controversy and debate that need further attention from the scientific community.
Journal ArticleDOI

Critical Examination of the Colloidal Particle Model of Globular Proteins

TL;DR: The findings point to limited validity of the colloidal protein model and to the need for further consideration and quantification of the effects of conformational changes on protein solution viscosity, protein association, and the phase behavior.
Journal ArticleDOI

The limitations of an exclusively colloidal view of protein solution hydrodynamics and rheology.

TL;DR: A minimal framework for models of crowded protein solution viscosity wherein critical protein-specific attributes (namely, conformation, surface hydration, and surface charge distribution) are addressed is defined.
Journal ArticleDOI

A Microliter Capillary Rheometer for Characterization of Protein Solutions

TL;DR: The development of a miniaturized capillary rheometer that meets the needs of the biopharamaceutical industry and is potentially scalable to a multiwell format is reported.
Journal ArticleDOI

Coarse-Grained Modeling of Antibodies from Small-Angle Scattering Profiles

TL;DR: The small-angle X-ray scattering profiles for a monoclonal antibody have been measured and the experimental compressibility curves can be accurately reproduced by an appropriate parametrization of the Baxter adhesive model, indicating the model provides a semiempirical equation of state for the antibody.