Proteins carry out the most difficult tasks in living cells. They do so by interacting specifically
with other molecules. This requires that they fold to a unique, globular conformation that is …

Over the past 15 years there has been an explosion of research on the dynamical properties
of proteins, largely driven by the emergence of a handful of techniques that are sensitive to …

Root mean-square deviation (RMSD) after roto-translational least-squares fitting is a
measure of global structural similarity of macromolecules used commonly. On the other …

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 …

The pK values of the titratable groups in ribonuclease Sa (RNase Sa)(pI= 3.5), and a charge-
reversed variant with five carboxyl to lysine substitutions, 5K RNase Sa (pI= 10.2), have …

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 ionizable groups in proteins with the lowest pKs are the carboxyl groups of aspartic acid
side-chains. One of the lowest, pK= 0.6, is observed for Asp76 in ribonuclease T1. This low …

Nuclear spin hyperpolarized water is utilized to obtain protein spectra not only in the folded
state but also during the refolding process. Polarization transfer to Ribonuclease Sa through …

RNase A self-associates under certain conditions to form a series of domain-swapped
oligomers. These oligomers show high catalytic activity against double-stranded RNA and …

Abstract Ribonuclease Sa (RNase Sa) contains no tryptophan (Trp) residues. We have
added single Trp residues to RNase Sa at sites where Trp is found in four other microbial …