Thermodynamics of unfolding of the all beta-sheet protein interleukin-1 beta.


Abstract

The thermal denaturation of interleukin-1 beta in solution has been studied by differential scanning calorimetry at various pH values. It is shown that the thermal transition of interleukin-1 beta is completely reversible below pH 2.5, only partly reversible in the pH range 2.5-3.5, and irreversible above pH 3.5. Analysis of the reversible unfolding of interleukin-1 beta shows that the heat denaturation is well approximated by a two-state transition and is accompanied by a significant increase of heat capacity. The partial heat capacity of denatured interleukin-1 beta is very close to that expected for the completely unfolded protein. This permitted us to assign the thermodynamic characteristics of interleukin-1 beta denaturation to its complete unfolding and to correlate them with structural features of the protein. The contributions of hydrogen bonding and hydrophobic interactions to the stability of interleukin-1 beta are analyzed and compared to those for other globular proteins. It is shown that the Gibbs energy of a hydrogen bond in a beta-sheet structure is greater than in alpha-helices. Study holds ProTherm entries: 4510, 4511, 4512, 4513, 4514 Extra Details:

Submission Details

ID: 9ANfwVXC

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:25 p.m.

Version: 1

Publication Details
Makhatadze GI;Clore GM;Gronenborn AM;Privalov PL,Biochemistry (1994) Thermodynamics of unfolding of the all beta-sheet protein interleukin-1 beta. PMID:8049234
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 PDB Entries

Structure ID Release Date Resolution Structure Title
1HIB 1993-03-29T00:00:00+0000 2.4 THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION
1I1B 1989-12-05T00:00:00+0000 2.0 CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-1BETA AT 2.0 ANGSTROMS RESOLUTION
1IOB 1996-03-14T00:00:00+0000 2.0 INTERLEUKIN-1 BETA FROM JOINT X-RAY AND NMR REFINEMENT
1ITB 1997-01-15T00:00:00+0000 2.5 TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
1L2H 2002-02-21T00:00:00+0000 1.54 Crystal structure of Interleukin 1-beta F42W/W120F mutant
1S0L 2003-12-31T00:00:00+0000 2.34 Interleukin 1 beta mutant F42W
1T4Q 2004-04-30T00:00:00+0000 2.1 Interleukin 1 beta F101W
1TOO 2004-06-14T00:00:00+0000 2.1 Interleukin 1B Mutant F146W
1TP0 2004-06-15T00:00:00+0000 2.2 Triple mutation in interleukin 1 beta cavity:replacement of phenylalanines with tryptophan.
1TWE 2004-06-30T00:00:00+0000 2.1 INTERLEUKIN 1 BETA MUTANT F101Y

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
94.8 Interleukin-1 beta P46648 IL1B_CERAT
95.4 Interleukin-1 beta P79182 IL1B_MACFA
95.4 Interleukin-1 beta P51493 IL1B_MACNE
96.1 Interleukin-1 beta P48090 IL1B_MACMU
100.0 Interleukin-1 beta P01584 IL1B_HUMAN