The thermal denaturation of bovine beta-lactoglobulin B was investigated by high-sensitivity differential scanning microcalorimetry between pH 1.5 and 3.0 in 20 mM phosphate buffer. The process was found to be a reversible, two-state transition. Progressive addition of guanidine hydrochloride at pH 3.0 leads to the appearance of a low-temperature calorimetric endotherm, corresponding to the cold renaturation of the protein. Circular dichroism experiments have confirmed the low and high temperature denaturation processes, and have shown some structural differences between both denatured states of beta-lactoglobulin B. Study holds ProTherm entries: 10123 Extra Details: Heat and cold denaturation of beta-lactoglobulin B. beta-lactoglobulin B; thermal stability; cold denaturation,guanidine hydrochloride; scanning calorimetry; circular dichroism
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:39 p.m.
|Number of data points||1|
|Proteins||Beta-lactoglobulin ; Beta-lactoglobulin|
|Assays/Quantities/Protocols||Experimental Assay: Tm|
|Libraries||Mutations for sequence LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI|