Domains in bovine seminal ribonuclease

Autor: Giuseppe Graziano, Francesca Catanzano
Rok vydání: 2007
Předmět:
Zdroj: Journal of Thermal Analysis and Calorimetry. 91:61-66
ISSN: 1572-8943
1388-6150
DOI: 10.1007/s10973-007-8537-2
Popis: Bovine seminal ribonuclease is the only pancreatic-type ribonuclease to possess a dimeric structure: the two identical subunits are covalently linked by two disulfide bridges. Actually, the protein exists in two different dimeric structures owing to the possibility of swapping the N-terminal α-helical segments: the swapped MxM dimer, and the non-swapped M=M dimer. The thermal denaturation of the two separated forms is investigated by differential scanning calorimetry. The process is reversible and can be represented by two sequential two-state transitions, indicating the presence of two domains in BS-RNase, regardless of the swapping phenomenon. Inspection of the structural models leads to the tentative identification of an external domain and a core domain, the latter more stable.
Databáze: OpenAIRE
Externí odkaz: