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2000
Volume 9, Issue 2
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Atomic Force Microscopy (AFM) has been a useful tool for molecular surface analysis and to estimate topographical properties of proteins. Here we report a topographical study of a chymotrypsin inhibitor from Schizolobium parahyba seeds (SPCI) by AFM. The underlying structure of SPCI oligomers has been resolved in nanometer order resolution. SPCI oligomerize in hexagonal, ellipsoid, comet, pyramidal, and “Z“ shaped. The hexagonal was the most observed oligomer shape.

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/content/journals/ppl/10.2174/0929866023408823
2002-04-01
2025-09-02
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/content/journals/ppl/10.2174/0929866023408823
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  • Article Type:
    Review Article
Keyword(s): afm; kunitz inhibitor; oligomer shape; spci; topography
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