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Article

Direct single-molecule observation of a protein living in two opposed native structures.

Proceedings of the National Academy of Sciences of the United States of America - 23 Jun 2009

Gambin Yann, Schug Alexander, Lemke Edward A, Lavinder Jason J, Ferreon Allan Chris M, Magliery Thomas J, Onuchic José N, Deniz Ashok A

Abstract excerpt

Biological activity in proteins requires them to share the energy landscape for folding and global conformational motions, 2 key determinants of function. Although most structural studies to date have focused on fluctuations around a single structural basin, we directly observe the coexistence of 2 symmetrically opposed conformations for a mutant of the Rop-homodimer (Repressor of Primer) in single-molecule...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19506258
DOI: 10.1073/pnas.0904461106
PMCID: PMC2700882

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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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