Lactoperoxidase consists of domains: a scanning calorimetric study.
Abstract
Thermal unfolding of lactoperoxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7) was studied by means of differential scanning calorimetry and optical methods. The protein consists of at least two domains differing in thermostability. The prosthetic group belongs to the domain of lower thermostability. Thermodynamic parameters of protein unfolding are given and found to be similar to corresponding data for globular proteins. Study holds ProTherm entries: 7311, 7312, 7313, 7314, 7315, 7316, 7317, 7318, 7319, 7320 Extra Details: hydrogen-peroxide oxidoreductase; optical method; domain;,prosthetic group
Submission Details
ID: C2ZBaVmA4
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:33 p.m.
Version: 1
Publication Details
Pfeil W;Ohlsson PI,Biochim. Biophys. Acta (1986) Lactoperoxidase consists of domains: a scanning calorimetric study. PMID:3730397Additional Information
Study Summary
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Data Distribution
Studies with similar sequences (approximate matches)