Both rat liver and Escherichia coli rRNA in 0.1M-sodium chloride were titrated with acid or alkali over the range pH 3-7 at approx. 0°C. rRNA did not bind acid reversibly and hysteresis was observed, i.e. the plot of acid bound to rRNA against pH had the form of a loop showing that the amount of acid bound at a particular pH depended on the direction of the titration. Although the boundary curv...

The therapeutic activity of peptides or protein drugs is highly dependent on their conformational structure. The protein structure is flexible and responds to external conditions, which may compromise the protein’s native conformation and influence its physical and chemical stability. The physical and chemical stability of peptides or protein drugs are important characteristics of biopharmaceut...

The “thermodynamic” hypothesis of protein conformation (1) states that the sequence of amino acids characteristic of a given protein is sufficient to determine its secondary and tertiary structure, for the molecule will assume the conformation thermodynamically most stable. In an analogous vein, the “conformation” hypothesis (2) proposes that the steric and noncovalent bonding properties of pol...

The physical basis for high-affinity interactions involving proteins is complex and potentially involves a range of energetic contributions. Among these are changes in protein conformational entropy, which cannot yet be reliably computed from molecular structures. We have recently used changes in conformational dynamics as a proxy for changes in conformational entropy of calmodulin upon associa...