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Surface characterization of proteins using multi-fractal property of heat-denatured aggregates BACK TO CONTENTS PDF PREVIOUS NEXT
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Title

 

 

 

 

Surface characterization of proteins using multi-fractal property of heat-denatured aggregates

 

Authors

Tapobrata Lahiri1, *, Hrishikesh Mishra1, Subrata Sarkar1, Krishna Misra2

 

Affiliation

1Indian Institute of Information Technology, Allahabad, India; 2Centre of Biotechnology, University of Allahabad, Allahabad, India

 

Email

tlahiri@iiita.ac.in; * Corresponding author

 

Article Type

Hypothesis

 

Date

received March 07, 2008; revised May 05, 2008; accepted May 31, 2008; published June 23, 2008

 

Abstract

Multi-fractal property of heat-denatured protein aggregates (HDPA) is characteristic of its individual form. The visual similarity between digitally generated microscopic images of HDPA with that of surface-image of its individual X-ray structures in protein databank (PDB) displayed using Visual Molecular Dynamics (VMD) viewer is basis of the study. We deigned experiments to view the fractal nature of proteins at different aggregate scales. Intensity based multi-fractal dimensions (ILMFD) extracted from various planes of digital microscopic images of protein aggregates were used to characterize HDPA into different classes. Moreover, the ILMFD parameters extracted from aggregates show similar classification pattern to digital images of protein surface displayed by VMD viewer using PDB entry. We discuss the use of irregular patterns of heat-denatured aggregate proteins to understand various surface properties in native proteins.

 

Keywords

protein structure; multi-fractal dimension; protein aggregate; digital image processing; light microscopy; degree of differentiation; graphical pair-wise class comparison

 

Citation

Lahiri et al., Bioinformation 2(9): 379-383 (2008)

 

Edited by

P. Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

Copyright

Publisher

 

Copyright Transfer Agreement

The authors of published articles in Bioinformation automatically transfer the copyright to the publisher upon formal acceptance. However, the authors reserve right to use the information contained in the article for non commercial purposes.

 

License

This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.