Lysozyme folds through two competing pathways. A fast pathway leads directly from a collapsed state to the native protein, whereas folding on a slow pathway proceeds through a partially folded intermediate (I(1)). At NaCl concentrations above 100 mM, a second transient intermediate (I(2)) is induced as judged by the appearance of an additional apparent rate constant in the refolding kinetics. Monitoring the time course of native molecules and of both intermediates shows that the NaCl-induced state (I(2)) is located on neither of the two folding pathways observed at low-salt concentrations. These results suggest that I(2) is a metastable high-energy intermediate at low-ionic strength and is located on a third folding pathway. The folding landscape of lysozyme seems to be complex with several high-energy intermediates located on parallel folding routes. However, the experiments show no evidence for partially folded states on the fast direct pathway. Study holds ProTherm entries: 16299, 16300, 16301 Extra Details: folding kinetics, new parallel pathway, lysozyme
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:47 p.m.
|Number of data points||6|
|Proteins||Lysozyme C ; Lysozyme C|
|Assays/Quantities/Protocols||Experimental Assay: m temp:10.0 C, ionic:NaCl: 0.85 M ; Experimental Assay: dG_H2O temp:10.0 C, ionic:NaCl: 0.85 M ; Experimental Assay: m temp:20.0 C, ionic:NaCl: 0.85 M ; Experimental Assay: dG_H2O temp:20.0 C, ionic:NaCl: 0.85 M ; Experimental Assay: m temp:20.0 C, ionic:: ; Experimental Assay: dG_H2O temp:20.0 C, ionic::|
|Libraries||Mutations for sequence KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL|
|Percent Identity||Matching Chains||Protein||Accession||Entry Name|