Title : Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy.

Pub. Date : 1996 Dec 10

PMID : 8961946






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1 Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. Urea ribonuclease A family member 1, pancreatic Homo sapiens
2 Therefore, our kinetic infrared studies provide evidence for a high structural similarity of urea-denatured and heat-denatured RNase A, corroborating the conclusions derived from the direct comparison of the infrared spectra of thermally and chemically denatured RNase A under equilibrium conditions [Fabian, H., & Mantsch, H.H. Urea ribonuclease A family member 1, pancreatic Homo sapiens
3 In detail, the kinetic infrared data demonstrate that in the time window of 0.1-30 s approximately 40% of the native beta-sheet structure in RNase A is formed in the presence of 0.6 M urea at pH* 3.6, indicating that up to 60% of the beta-structure is formed out of the time window used in this study. Urea ribonuclease A family member 1, pancreatic Homo sapiens