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Cited by 307

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Experimental Identification of Downhill Protein Folding

Garcia-Mira, Maria M., Sadqi, Mourad, Fischer, Niels, Sanchez-Ruiz, Jose M., Muñoz, Victor·2002·Science

Abstract

Theory predicts the existence of barrierless protein folding. Without barriers, folding should be noncooperative and the degree of native structure should be coupled to overall protein stability. We investigated the thermal unfolding of the peripheral subunit binding domain from Escherichia coli 's 2-oxoglutarate dehydrogenase multienzyme complex (termed BBL) with a combination of spectroscopic techniques and calorimetry. Each technique probed a different feature of protein structure. BBL has a defined three-dimensional structure at low temperatures. However, each technique showed a distinct unfolding transition. Global analysis with a statistical mechanical model identified BBL as a downhill-folding protein. Because of BBL's biological function, we propose that downhill folders may be molecular rheostats, in which effects could be modulated by altering the distribution of an ensemble of structures.

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Metadata

Authors
Garcia-Mira, M. M., Sadqi, M., Fischer, N., Sanchez-Ruiz, J. M., & Muñoz, V.
Venue
Science
Published
2002-12-13
Volume
298
Issue
5601
Pages
2191-2195
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2096599403
Cited by
307
References
2
FWCI
5.29
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Experimental Identification of Downhill Protein Folding. https://app.cochat.ai/papers/10.1126/science.1077809
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Garcia-Mira, M. M., Sadqi, M., Fischer, N., Sanchez-Ruiz, J. M., & Muñoz, V. (2002). Experimental Identification of Downhill Protein Folding. Science. https://doi.org/10.1126/science.1077809

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.