Topographical Analysis of Schizolobium Parahyba Chymotrypsin Inhibitor (Spci) by Atomic Force Microscopy

Authors: Jose Roberto S.A. Leite¹; Luciano P. Silva¹; Clarice C.u.n.h.a. Taveira¹; Rozeni C.L. Teles¹; Sonia M. de Freitas¹; Ricardo B.e.n.t.e.s. Azevedo¹

Source: Protein and Peptide Letters, Volume 9, Number 2, April 2002 , pp. 179-184(6)

Publisher: Bentham Science Publishers

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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.

Keywords: spci; topography; oligomer shape; afm; kunitz inhibitor

Document Type: Review article

DOI: 10.2174/0929866023408823

Affiliations: 1: Laboratorio de Morfologia e Morfogenese, Departamento de Genetica e Morfologia, Universidade de Brasilia,Brasilia, DF, Brazil.

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