Title : Hydrogen exchange in ribonuclease A and ribonuclease S: evidence for residual structure in the unfolded state under native conditions.

Pub. Date : 1999 Jan 15

PMID : 9878434






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Two-dimensional NMR spectroscopy has been used to monitor the exchange of backbone amide protons in ribonuclease A (RNase A) and its subtilisin-cleaved form, ribonuclease S (RNase S). Amides ribonuclease A family member 1, pancreatic Homo sapiens
2 Two-dimensional NMR spectroscopy has been used to monitor the exchange of backbone amide protons in ribonuclease A (RNase A) and its subtilisin-cleaved form, ribonuclease S (RNase S). Amides ribonuclease A family member 1, pancreatic Homo sapiens
3 For the amide protons of a large number of residues in RNase A, the free energies at 25 degreesC for exchange competent unfolding processes are much lower than the calorimetric denaturation free energies, thus showing that exchange occurs through local fluctuations in the native state. Amides ribonuclease A family member 1, pancreatic Homo sapiens