Amide H/D exchange in the thermal transition of bovine pancreatic ribonuclease A.

The H/D exchange behavior of RNase A at pH 2.5 at a number of temperatures spanning the thermal transition region has been examined by NMR spectroscopy. The amide proton of V116 has a slow rate of H/D exchange even at temperatures above the midpoint of the thermal transition. The H/D exchange behavior of the peptide corresponding to residues 105-124 of RNase A and the peptide corresponding to residues 115-117 is compared with that of RNase A, showing that folding/unfolding cannot be described by a two-state model, and that both short- and long-range interactions are responsible for the slow rate of H/D exchange.