Heat denaturation of human orosomucoid in water/methanol mixtures.


Abstract

Heat denaturation of orosomucoid in solutions of methanol concentrations ranging from 0 to 70% (v/v) has been studied by using circular dichroism, intrinsic protein fluorescence and thermal difference absorption spectroscopy. Regardless of its high saccharide content (40%), the highly cooperative denaturation transition of orosomucoid is fully reversible in neutral water solution. A two-state model has been successfully applied; the numerical analysis results in thermodynamical parameter values that are in close agreement with previously reported experimental data from calorimetric measurements. However, in solutions containing even minute concentrations of methanol (5%) the heat denaturation is irreversible. After cooling of the denatured protein the refolded molecules exhibit a higher alpha-helical content than the native one. Possibilities of methanol interaction with native and denatured protein molecule are discussed. Study holds ProTherm entries: 9372 Extra Details: orosomucoid; alpha1-acid glycoprotein; denaturation; circular dichroism; fluorescence

Submission Details

ID: CCSZZMU7

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:37 p.m.

Version: 1

Publication Details
Kodícek M;Infanzón A;Karpenko V,Biochim. Biophys. Acta (1995) Heat denaturation of human orosomucoid in water/methanol mixtures. PMID:7811724
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
3KQ0 2010-02-02 1.8 Crystal structure of human alpha1-acid glycoprotein

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Alpha-1-acid glycoprotein 1 P02763 A1AG1_HUMAN