On the cooperativity of the thermal denaturation of mini-proteins |
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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: | It is well established that the reversible thermal denaturation of small globular proteins is a cooperative two-state transition,
analogous to a first-order phase transition in a finite-size system. Finite-size effects on the cooperativity of the reversible
thermal denaturation become more important when the polypeptide chain is very small, as in the case of some synthesized mini-proteins.
The analysis of two specific examples of mini-proteins, by means of a statistical mechanical approach, leads to the conclusion
that their thermal denaturation, in view of its broadness and energetics, cannot be considered a cooperative first-order phase
transition. |
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Keywords: | cooperativity differential scanning calorimetry finite-size effects first-order phase transition mini-proteins two-state model |
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