The contribution of specific packing to the stability of the sperm whale apomyoglobin intermediate has been studied by urea denaturation monitored by circular dichroism and fluorescence. Mutations disrupting native packing sites within the subdomain formed by the A, G and H helices destabilize the intermediate, in contrast to the conclusion drawn from earlier studies of pH-induced unfolding. Based on these results, the intermediate is proposed to be stabilized by both partially formed native-like tertiary, and non-specific hydrophobic interactions forming a subdomain folding intermediate. The results help to explain how the intermediate acquires its structure and stability. Study holds ProTherm entries: 2091, 2092, 2093, 2094, 2095, 2096, 2097, 2098, 2099, 2812, 2813, 2814, 2815, 2816, 2817, 2818, 2819, 2820, 2821, 2822, 2823, 2824, 2825, 2826, 2827, 2828, 2829 Extra Details: the transition is 3-state apomyglobin; specific packing; hydrophobic interactions;,stability; folding
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:18 p.m.
|Number of data points||54|
|Proteins||Myoglobin ; Myoglobin|
|Assays/Quantities/Protocols||Experimental Assay: dG ; Derived Quantity: ddG|
|Libraries||Mutations for sequence VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG|