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The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
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2009 (Engelska)Ingår i: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 106, nr 51, s. 21619-21624Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

An increasing number of protein structures are found to encompass multiple folding nuclei, allowing their structures to be formed by several competing pathways. A typical example is the ribosomal protein S6, which comprises two folding nuclei (sigma1 and sigma2) defining two competing pathways in the folding energy landscape: sigma1 --> sigma2 and sigma2 --> sigma1. The balance between the two pathways, and thus the order of folding events, is easily controlled by circular permutation. In this study, we make use of this ability to manipulate the folding pathway to demonstrate that the dynamic motions of the S6 structure are independent of how the protein folds. The HD-exchange protection factors remain the same upon complete reversal of the folding order. The phenomenon arises because the HD-exchange motions and the high-energy excitations controlling the folding pathway occur at separated free-energy levels: the Boltzmann distribution of unproductive unfolding attempts samples all unfolding channels in parallel, even those that end up in excessively high barriers. Accordingly, the findings provide a simple rationale for how to interpret native-state dynamics without the need to invoke fluctuations off the normal unfolding reaction coordinate.

Ort, förlag, år, upplaga, sidor
2009. Vol. 106, nr 51, s. 21619-21624
Nyckelord [en]
circular permutation, energy landscape, protein dynamics, transition state
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Kemi
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URN: urn:nbn:se:umu:diva-30253DOI: 10.1073/pnas.0907665106ISI: 000272994200030PubMedID: 19966220OAI: oai:DiVA.org:umu-30253DiVA, id: diva2:281192
Tillgänglig från: 2009-12-15 Skapad: 2009-12-15 Senast uppdaterad: 2018-06-08Bibliografiskt granskad

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