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Article

Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A.

Proceedings of the National Academy of Sciences of the United States of America - 21 Dec 2004

Welker Ervin, Maki Kosuke, Shastry M C Ramachandra, Juminaga Darmawi, Bhat Rajiv, Scheraga Harold A, Roder Heinrich

Abstract excerpt

The earliest folding events in single-tryptophan mutants of RNase A were investigated by fluorescence measurements by using a combination of stopped-flow and continuous-flow mixing experiments covering the time range from 70 micros to 10 s. An ultrarapid double-jump mixing protocol was used to study refolding from an unfolded ensemble containing only native proline isomers. The continuous-flow measurements...

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Identifiers

PMID: 15574490
DOI: 10.1073/pnas.0407999101
PMCID: PMC539777

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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