Conformation, stability, and folding of interleukin 1 beta.


Recombinant human interleukin 1 beta has been studied in solution with respect to its conformation, stability, and characteristics of unfolding and refolding. It is an all-beta-type, stable globular protein with a high cooperativity under conditions where refolding is reversible. The tryptophan residue is approximately 40% exposed to solvent, and the four tyrosines are 50% exposed. The fluorescence of the single tryptophan residue is quenched at pH 7.5 but dequenched by high salt, by titration to lower pH with a pK of 6.59, and by denaturants, resulting in an unusual biphasic change in fluorescence on unfolding. Both histidine and thiol residues have been excluded as being responsible for the pH dependence of fluorescence by site-directed mutagenesis and by chemical modification, respectively. The likely candidate is an aspartate or glutamate. Study holds ProTherm entries: 3866 Extra Details: all-beta-type; cooperativity ; biphasic change;,chemical modification

Submission Details

ID: yFsipxN

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:23 p.m.

Version: 1

Publication Details
Craig S;Schmeissner U;Wingfield P;Pain RH,Biochemistry (1987) Conformation, stability, and folding of interleukin 1 beta. PMID:3498512
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 Interleukin-1 beta P01584 IL1B_HUMAN
96.1 Interleukin-1 beta P48090 IL1B_MACMU
95.4 Interleukin-1 beta P51493 IL1B_MACNE
95.4 Interleukin-1 beta P79182 IL1B_MACFA
94.8 Interleukin-1 beta P46648 IL1B_CERAT