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

Authors: Jose Roberto S.A. Leite; Luciano P. Silva; Clarice C.u.n.h.a. Taveira; Rozeni C.L. Teles; Sonia M. de Freitas; Ricardo B.e.n.t.e.s. Azevedo

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: http://dx.doi.org/10.2174/0929866023408823

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

Publication date: 2002-04-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.