Heat denaturation of pepsinogen in a water-ethanol mixture.
Abstract
The effect of ethanol and pH on thermodynamic parameters and cooperativity of pepsinogen heat denaturation was studied by scanning microcalorimetry. Addition of 20% ethanol decreases the protein denaturation temperature by 10.7 degrees C at pH 6.4 and 15.8 degrees C at pH 8.0. It also decreases the denaturation heat capacity increment from 5.8 to 4.2 kcal/K.mol. The dependences of calorimetric denaturation enthalpy on denaturation temperature both in water and 20% ethanol are linear and intersect at about 95 degrees C. In 20% ethanol the pH shift from 5.9 to 8.0 results in a decreased number of cooperative domains in pepsinogen. This process causes no changes either in the secondary structure or in the local surroundings of aromatic amino acids. It is concluded that ethanol addition does not affect the cooperativity of pepsinogen denaturation substantially until the pH change provokes redistribution of charges in the protein molecule. Study holds ProTherm entries: 9828, 9829, 9830, 9831, 9832, 9833, 9834, 9835, 9836, 9837, 9838, 9839, 9840 Extra Details: pepsinogen; heat denaturation; ethanol; scanning microcalorimetry
Submission Details
ID: eiChr5fS3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:38 p.m.
Version: 1
Publication Details
Makarov AA;Protasevich II;Bazhulina NP;Esipova NG,FEBS Lett. (1995) Heat denaturation of pepsinogen in a water-ethanol mixture. PMID:8001679Additional 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 |
|---|
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 |
|---|---|---|---|
| 1F34 | 2000-05-31T00:00:00+0000 | 2.45 | CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN |
| 1PSA | 1991-10-22T00:00:00+0000 | 2.9 | STRUCTURE OF A PEPSIN(SLASH)RENIN INHIBITOR COMPLEX REVEALS A NOVEL CRYSTAL PACKING INDUCED BY MINOR CHEMICAL ALTERATIONS IN THE INHIBITOR |
| 1YX9 | 2005-02-20T00:00:00+0000 | 3.0 | Effect of Dimethyl Sulphoxide on the crystal structure of Porcine Pepsin |
| 2PSG | 1991-01-23T00:00:00+0000 | 1.8 | REFINED STRUCTURE OF PORCINE PEPSINOGEN AT 1.8 ANGSTROMS RESOLUTION |
| 3PEP | 1989-10-24T00:00:00+0000 | 2.3 | REVISED 2.3 ANGSTROMS STRUCTURE OF PORCINE PEPSIN. EVIDENCE FOR A FLEXIBLE SUBDOMAIN |
| 3PSG | 1991-09-03T00:00:00+0000 | 1.65 | THE HIGH RESOLUTION CRYSTAL STRUCTURE OF PORCINE PEPSINOGEN |
| 4PEP | 1989-12-18T00:00:00+0000 | 1.8 | THE MOLECULAR AND CRYSTAL STRUCTURES OF MONOCLINIC PORCINE PEPSIN REFINED AT 1.8 ANGSTROMS RESOLUTION |
| 5PEP | 1990-05-30T00:00:00+0000 | 2.34 | X-RAY ANALYSES OF ASPARTIC PROTEASES. II. THREE-DIMENSIONAL STRUCTURE OF THE HEXAGONAL CRYSTAL FORM OF PORCINE PEPSIN AT 2.3 ANGSTROMS RESOLUTION |
| 6XCT | 2020-06-09T00:00:00+0000 | 1.99 | Porcine pepsin in complex with amprenavir |
| 6XCY | 2020-06-09T00:00:00+0000 | 2.05 | Porcine pepsin in complex with ritonavir |