Domains in bovine seminal ribonuclease |
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Authors: | Francesca Catanzano G Graziano |
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Institution: | (1) Dipartimento di Scienze Biologiche ed Ambientali, Università del Sannio, Via Port’Arsa 11, 82100 Benevento, Italy |
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Abstract: | 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. |
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Keywords: | differential scanning calorimetry domain swapping structural domain thermodynamic domain |
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