The folding pathway of an FF domain: Characterization of an on-pathway intermediate state under folding conditions by N-15, C-13(alpha) and C-13-methyl relaxation dispersion and H-1/(2) H-exchange NMR Spectroscopy

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MARC

Korzhnev, Dmitry M.University of Toronto, Ontario, Canada (author)

The folding pathway of an FF domain : Characterization of an on-pathway intermediate state under folding conditions by N-15, C-13(alpha) and C-13-methyl relaxation dispersion and H-1/(2) H-exchange NMR Spectroscopy

Article/chapterEnglish2007

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Elsevier,2007
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LIBRIS-ID:oai:DiVA.org:liu-85035
https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-85035URI
https://doi.org/10.1016/j.jmb.2007.06.012DOI

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Language:English
Summary in:English

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Subject category:ref swepub-contenttype
Subject category:art swepub-publicationtype

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The FF domain from the human protein HYPA/FBP11 folds via a lowenergy on-pathway intermediate (. Elucidation of the structure of such folding intermediates and denatured states under conditions that favour folding are difficult tasks. Here, we investigated the millisecond time-scale equilibrium folding transition of the 71-residue four-helix bundle wild-type protein by N-15, C-13(alpha) and methyl C-13 Carr-Purcell-Meiboom-Gill (CPMG) NMR relaxation dispersion experiments and by H-exchange measurements. The relaxation data for the wild-type protein fitted a simple two-site exchange process between the folded state (F) and I. Destabilization of F in mutants A17G and Q19G allowed the detection of the unfolded state U by 15N CPMG relaxation dispersion. The dispersion data for these mutants fitted a three-site exchange scheme, U-I-F, with I populated higher than U. The kinetics and thermodynamics of the folding reaction were obtained via temperature and urea-dependent relaxation dispersion experiments, along with structural information on I from backbone N-15, C-13(alpha) and side-chain methyl 13C chemical shifts, with further information from protection factors for the backbone amide groups from H-1/(2) H-exchange. Notably, helices H1-H3 are at least partially formed in 1, while helix H4 is largely disordered. Chemical shift differences for the methyl 13 C nuclei suggest a paucity of stable, native-like hydrophobic interactions in 1. These data are consistent with (D-analysis of the rate-limiting transition state between I and F. The combination of relaxation dispersion and (1) data can elucidate whole experimental folding pathways.

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Religa, Tomasz L.MRC, University of Cambridge, UK (author)
Lundström, Patrik,1971-University of Toronto, ON, Canada(Swepub:liu)patlu71 (author)
Fersht, Alan R.MRC, University of Cambridge, UK (author)
Kay, Lewis E.University of Toronto, Ontario, Canada (author)
University of Toronto, Ontario, CanadaMRC, University of Cambridge, UK (creator_code:org_t)

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In:Journal of Molecular Biology: Elsevier372:2, s. 497-5120022-28361089-8638

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