Poor protein solubility is a common problem in high-resolution structural studies, formulation
of protein pharmaceuticals, and biochemical characterization of proteins. One popular …

Protein conformational stability is an important concern in many fields. Here, we describe a
strategy for significantly increasing conformational stability by optimizing β-turn sequence …

We previously suggested that proteins gain more stability from the burial and hydrogen
bonding of polar groups than from the burial of nonpolar groups (Pace, CN (2001) …

The net charge and isoelectric pH (pI) of a protein depend on the content of ionizable groups
and their pK values. Ribonuclease Sa (RNase Sa) is an acidic protein with a pI= 3.5 that …

The aim of this study was to gain a better understanding of the contribution of hydrogen
bonds by tyrosine-OH groups to protein stability. The amino acid sequences of RNases Sa …

Protein solubility is a problem for many protein chemists, including structural biologists and
developers of protein pharmaceuticals. Knowledge about how intrinsic factors influence …

Osmolytes stabilize proteins to thermal and chemical denaturation. We have studied the
effects of the osmolytes sarcosine, betaine, trimethylamine-N-oxide, and taurine on the …

High concentration protein delivery is difficult to achieve for several protein pharmaceuticals
due to low solubility. In this review, we discuss different types of low protein solubility …

The hydrophobic effect is widely believed to be an important determinant of protein stability.
However, it is difficult to obtain unambiguous experimental estimates of the contribution of …

Recent work has shown that, with synthetic analogues of C‐peptide (residues 1–13 of
ribonuclease A), the stability of the peptide helix in H2O depends strongly on the charge on …