Title : NMR study of the cold, heat, and pressure unfolding of ribonuclease A.

Pub. Date : 1995 Jul 11

PMID : 7612603

1 Functional Relationships(s)
Compound Name
Protein Name
1 The appearance of a new histidine resonance in the cold-denatured and pressure-denatured RNase A spectra, compared to the absence of this resonance in the heat-denatured state, indicates that the pressure-denatured and cold-denatured states may contain partially folded structures that are similar to that of the early folding intermediate found in the temperature-jump experiment reported by Blum et al. Histidine ribonuclease A family member 1, pancreatic Homo sapiens