Title : Initial hydrophobic collapse is not necessary for folding RNase A.

Pub. Date : 1998

PMID : 9562551






2 Functional Relationships(s)
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1 RESULTS: In this study, we investigate the refolding of chemically denatured, disulfide-intact ribonuclease A (RNase A) by monitoring compaction and secondary structure formation using stopped-flow dynamic light scattering and stopped-flow CD, respectively. Disulfides ribonuclease A family member 1, pancreatic Homo sapiens
2 RESULTS: In this study, we investigate the refolding of chemically denatured, disulfide-intact ribonuclease A (RNase A) by monitoring compaction and secondary structure formation using stopped-flow dynamic light scattering and stopped-flow CD, respectively. Disulfides ribonuclease A family member 1, pancreatic Homo sapiens