Many bioprocess separations involve manipulating the solution conditions to selectively
remove or concentrate a target protein. The selectivity is determined by the thermodynamics …

Membrane proteins represent roughly one-third of the proteins encoded in the genome, yet
fewer than 1% of the proteins are of known structure. High-throughput crystallography offers …

We studied the non‐native aggregation of recombinant human granulocyte stimulating factor
(rhGCSF) in solution conditions where native rhGCSF is both conformationally stable …

Better predictive ability of salt and buffer effects on protein–protein interactions requires
separating out contributions due to ionic screening, protein charge neutralization by ion …

Intraneuronal deposition of α-synuclein as fibrils and oxidative stress are both implicated in
the pathogenesis of Parkinson's disease. We found that the critical rate-limiting step in …

Protein aggregation is broadly important in diseases and in formulations of biological drugs.
Here, we develop a theoretical model for reversible protein–protein aggregation in salt …

Abstract Preface; 1. Introduction; 2. Globular protein structure; 3. Experimental methods; 4.
Thermodynamics and statistical mechanics; 5. Protein-protein interactions; 6. Theoretical …

Nucleation of ordered solid phases of proteins triggers numerous phenomena in laboratory,
industry, and in healthy and sick organisms. Recent simulations and experiments with …

Understanding interactions and phase transitions in protein solutions is essential in order to
develop systematic protein crystallisation strategies. Recent studies show that proteins near …

Recent studies of globular protein solutions have uniformly adopted a colloidal view of
proteins as particles, a perspective that neglects the polymeric primary structure of these …