An experimental investigation of conformational fluctuations in proteins G and L

Richard B. Tunnicliffe, Joe L. Waby, Ryan J. Williams, Mike P. Williamson

    Research output: Contribution to journalArticlepeer-review


    The B1 domains of streptococcal proteins G and L are structurally similar, but they have different sequences and they fold differently. We have measured their NMR spectra at variable temperature using a range of concentrations of denaturant. Many residues have curved amide proton temperature dependence, indicating that they significantly populate alternative, locally unfolded conformations. The results, therefore, provide a view of the locations of low-lying, locally unfolded conformations. They indicate approximately 4-6 local minima for each protein, all within ca. 2.5 kcal/mol of the native state, implying a locally rough energy landscape. Comparison with folding data for these proteins shows that folding involves most molecules traversing a similar path, once a transition state containing a β hairpin has been formed, thereby defining a well-populated pathway down the folding funnel. The hairpin that directs the folding pathway differs for the two proteins and remains the most stable part of the folded protein. ©2005 Elsevier Ltd. All rights reserved.
    Original languageEnglish
    Pages (from-to)1677-1684
    Number of pages7
    Issue number11
    Publication statusPublished - Nov 2005


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