Journal of Biosciences

, Volume 8, Issue 1–2, pp 57–66 | Cite as

Hierarchic organization of globular proteins: Experimental studies on thermolysin

  • Angelo Fontana
  • Claudio Vita
  • Daniele Dalzoppo


Previous studies from this laboratory have shown that the thermolysin fragment 121–316, comprising entirely the“all-α” COOH-terminal structural domain 158–316, as well as fragment 206–316 (fragment FII) are able to refold into a native-like, stable structure independently from the rest of the protein molecule. The present report describes conformational properties of fragments 228–316 and 255–316 obtained by chemical and enzymatic cleavage of fragment FII, respectively. These subfragments are able to acquire a stable conformation of native-like characteristics, as judged by quantitative analysis of secondary structure from far-ultra-violet circular dichroism spectra and immunochemical properties using rabbit anti-thermolysin antibodies. Melting curves of the secondary structure of the fragments show cooperativity with a temperature of half-denaturationTmof 65–66°C. The results of this study provide evidence that it is possible to isolate stable supersecondary structures (folding units) of globular proteins and correlate well with predictions of subdomains of the COOH-terminal structural domain 158–316 of thermolysin.


Circular dichroism immunochemistry protein domains protein fragments thermolysin 

Abbreviation used


Circular dichroism


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Copyright information

© Indian Academy of Sciences 1985

Authors and Affiliations

  • Angelo Fontana
    • 1
  • Claudio Vita
    • 1
  • Daniele Dalzoppo
    • 1
  1. 1.Institute of Organic Chemistry,Biopolymer Research Centre of CNRUniversity of PaduaPaduaItaly

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