【摘 要】
：
Nowadays there is a strong interest in partly folded or even fully disordered proteins,since these protein states can have a role in the proper functioning
【机 构】
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CRIBIBiotechnologyCentreUniversityofPaduaItaly
【出 处】
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2008中国深圳蛋白质和多肽科学大会
论文部分内容阅读
Nowadays there is a strong interest in partly folded or even fully disordered proteins,since these protein states can have a role in the proper functioning of proteins.However,the analysis of protein structural disorder is quite problematic and,to this aim,physicochemical and computational techniques for identifying and characterizing protein conformational disorder are being explored.In recent years,we have demonstrated that limited proteolysis experiments can be successfully used to probe conformational features of proteins.This approach relies on the fact that the sites of limited proteolysis along a polypeptide chain are characterised by enhanced backbone flexibility and,therefore,proteolytic probes can pinpoint the sites of local unfolding orprotein disorder in a protein chain.
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