Heat and cold denaturation of beta-lactoglobulin B.


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

Submission Details

ID: m53oWCjH

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:39 p.m.

Version: 1

Publication Details
Azuaga AI;Galisteo ML;Mayorga OL;Cortijo M;Mateo PL,FEBS Lett. (1992) Heat and cold denaturation of beta-lactoglobulin B. PMID:1516695
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Beta-lactoglobulin P02754 LACB_BOVIN
98.8 Beta-lactoglobulin P02755 LACB_BUBBU
96.3 Beta-lactoglobulin P02756 LACB_CAPHI
95.7 Beta-lactoglobulin P67976 LACB_SHEEP
95.7 Beta-lactoglobulin P67975 LACB_OVIMU