The thermal unfolding of hevein, a small disulfide-rich protein.


Abstract

Differential scanning calorimetry was used to study the thermal unfolding of hevein, a 43-residue disulfide-rich protein whose three-dimensional structure has been determined by X-ray diffraction. In the range pH 2.0-3.7 this process was approximately 75% reversible as judged by repeated scans on the same sample. The ratios of van'tr Hoff to calorimetric enthalpies were considerably larger than one, suggesting that intermolecular cooperation is involved in the unfolding of this protein. Alternatively, it is possible that the partial irreversibility of this process may cause distortions of the endotherm that affect the calculation of the van't Hoff enthalpy. Experimental changes in heat capacity and enthalpy were compared with those calculated from polar and nonpolar surface areas buried in the native state. It was found that when the unfolded state is represented as an extended chain without disulfide cross-links, experimental and calculated parameters agree well. However, if the unfolded protein is modeled with the presence of disulfide bridges, the agreement between the two sets of parameters is lost. The entropy change/residue at 112 degrees C is considerably smaller than the average value for globular proteins, thus suggesting that, as expected, disulfide bonds strongly influence the entropy of the unfolded state of this protein. Study holds ProTherm entries: 7614, 7615, 7616, 7617, 7618, 7619, 7620, 7621 Extra Details: hevein; disulfide-rich protein; thermal unfolding;,differential scanning caloriometry

Submission Details

ID: oju83KPF

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Hernández-Arana A;Rojo-Domínguez A;Soriano-García M;Rodríguez-Romero A,Eur. J. Biochem. (1995) The thermal unfolding of hevein, a small disulfide-rich protein. PMID:7737158
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
1HEV 1994-01-31 HEVEIN: THE NMR ASSIGNMENT AND AN ASSESSMENT OF SOLUTION-STATE FOLDING FOR THE AGGLUTININ-TOXIN MOTIF
1T0W 2004-09-28 25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina
4WP4 2015-03-04 1.43 Hev b 6.02 (hevein) extracted from surgical gloves
1Q9B 2004-01-13 1.5 CRYSTAL STRUCTURE ANALYSIS OF Hev b 6.02 (HEVEIN) AT 1.5 ANGSTROMS RESOLUTION
1WKX 2005-07-19 1.7 Crystal Structure of a Hev b 6.02 Isoallergen

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Pro-hevein P02877 HEVE_HEVBR