Unfolding profiles of two calcium-binding lysozymes, equine milk lysozyme and pigeon egg-white lysozyme, were obtained by circular dichroism and proton NMR measurements. Equine lysozyme unfolds through a stable molten globule intermediate. The molten globule of equine lysozyme was characterized as more ordered than that of bovine alpha-lactalbumin. On the other hand, pigeon lysozyme unfolds by a two-state mechanism and the intermediate could not be observed in guanidine or thermal unfolding, the same as with conventional non-calcium-binding lysozymes. Thus, from the point of view of the unfolding profile, equine lysozyme belongs to the group of alpha-lactalbumin, but pigeon lysozyme belongs to the conventional lysozyme group. Study holds ProTherm entries: 10366, 10367, 10368 Extra Details: Transition I calcium-binding lysozyme; alpha-lactalbumin; folding intermediate;,pigeon lysozyme; equine lysozyme
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:40 p.m.
|Number of data points||3|
|Proteins||Lysozyme C ; Lysozyme C, milk isozyme ; Lysozyme C, milk isozyme|
|Assays/Quantities/Protocols||Experimental Assay: Tm|
|Libraries||Mutations for sequence KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL ; Mutations for sequence KDIPRCELVKILRRHGFEGFVGKTVANWVCLVKHESGYRTTAFNNNGPNSRDYGIFQINSKYWCNDGKTRGSKNACNINCSKLRDDNIADDIQCAKKIAREARGLTPWVAWKKYCQGKDLSSYVRGC|