Distribution of charges in Bacillus intermedius 7P ribonuclease determines the number of cooperatively melting regions of the globule.
A correlation between the distribution of charged side groups in the globule of Bacillus intermedius 7P ribonuclease (binase) and the process of heat denaturation was studied at different pH values in order to estimate a relation between charge distribution in globular proteins and the character of cooperative thermodynamic transitions. As was shown by comparing the results of scanning microcalorimetric analysis of heat denaturation with the three-dimensional structure of binase, at optimal pH the molecule exists as a single cooperative system stabilized by hydrogen bonds, Van der Waals' contacts, and electrostatic interactions like salt bridges. At pH lower than 4.0 (below the physiological optimum) the cooperativity type of the system was found to change due to a reversible cooperative transition in the ternary structure of the protein globule. It has been concluded that the molecular architecture and the arrangement of atoms do not change considerably in different environments; thus the thermodynamic properties of the globule vary due to the alteration of charge distribution and the consequent changes in the size and number of cooperative regions of the globule. Thus, structural and energetic domains may be non-coincident in proteins.
Protasevich
I I
II
Institute of Molecular Biology, USSR Academy of Sciences, Moscow.
Platonov
A L
AL
Pavlovsky
A G
AG
Esipova
N G
NG
D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins; D002152:Calorimetry, Differential Scanning; D004722:Endoribonucleases; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D001426:Bacterial Proteins; D004722:Endoribonucleases; C022543:ribonuclease T(2)