Oligomerization states of Bowman-Birk inhibitor by atomic force microscopy and computational approaches

Several methods have been applied to study protein–protein interaction from structural and thermodynamic point of view. The present study reveals that atomic force microscopy (AFM), molecular modeling, and docking approaches represent alternative methods offering new strategy to investigate structur...

Full description

Saved in:
Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2005-11, Vol.61 (3), p.642-648
Main Authors: Silva, Luciano P., Azevedo, Ricardo B., Morais, Paulo C., Ventura, Manuel M., Freitas, Sonia M.
Format: Article
Language:English
Subjects:
accessible surface area
AFM
atomic force microscopy
Computational Biology
Dimerization
docking
Microscopy, Atomic Force
Protein Structure, Quaternary
proteinase inhibitor
Reproducibility of Results
self-assembly
Structure-Activity Relationship
Trypsin Inhibitor, Bowman-Birk Soybean - chemistry
Trypsin Inhibitor, Bowman-Birk Soybean - ultrastructure
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Several methods have been applied to study protein–protein interaction from structural and thermodynamic point of view. The present study reveals that atomic force microscopy (AFM), molecular modeling, and docking approaches represent alternative methods offering new strategy to investigate structural aspects in oligomerization process of proteinase inhibitors. The topography of the black‐eyed pea trypsin/chymotrypsin inhibitor (BTCI) was recorded by AFM and compared with computational rigid‐bodies docking approaches. Multimeric states of BTCI identified from AFM analysis showed globular–ellipsoidal shapes. Monomers, dimers, trimers, and hexamers were the most prominent molecular arrays observed in AFM images as evaluated by molecular volume calculations and corroborated by in silico docking and theoretical approaches. We therefore propose that BTCI adopts stable and well‐packed self‐assembled states in monomer–dimer–trimer–hexamer equilibrium. Although there are no correlation between specificity and packing efficiency among proteinases and proteinase inhibitors, the AFM and docked BTCI analyses suggest that these assemblies may exist in situ to play their potential function in oligomerization process. Proteins 2005. © 2005 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.20646