Interactions of urea with native and unfolded proteins: a volumetric study.
Toronto, Canada. In J Phys Chem B, 2014
We use this approach to analyze our urea-dependent data on the partial molar volume and adiabatic compressibility of lysozyme, apocytochrome c, ribonuclease A, and α-chymotrypsinogen A. The analysis produces the thermodynamic properties of elementary urea-protein association reactions while also yielding estimates of the effective solvent-accessible surface areas of the native and unfolded protein states.
Aggregates of α-chymotrypsinogen anneal to access more stable states.
Newark, United States. In Biotechnol Bioeng, 2014
Here it is shown that under mildly-denaturing conditions (elevated temperature or [urea]), where the native monomer (N) is slightly favored compared to the unfolded state (U), α-chymotrypsinogen A (aCgn) non-native aggregates undergo a structural relaxation or annealing process to reach even more stable states.
Protein entrapment in PEGylated lipid nanoparticles.
Châtenay-Malabry, France. In Int J Pharm, 2013
Nanoencapsulation of three cationic proteins (human brain-derived neurotrophic factor (BDNF), α-chymotrypsinogen A, and histone H3) was investigated using anionic nanoparticle (NP) carriers.