Protein sequence complexity revisited. Relationship with fractal 3D structure, topological and kinetic parameters

• Type: Article in International Scientific Journal
• Date: 2014

Authors

Tejera, E (Author) Other; Nieto Villar, J (Author) Other; Rebelo, I (Author) FFUP

Journal

Title: Physica A: Statistical Mechanics and its Applications

Vol. 410

Pages: 287-301

ISSN: 0378-4371

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 1 Citation

Scopus - 1 Citation

Scientific classification

FOS: Natural sciences > Physical sciences

Other information

Authenticus ID: P-009-HC4

DOI: 10.1016/j.physa.2014.05.019

Abstract (EN): The study of protein sequence complexity is not a new area and several methodological approaches are available in order to describe or represent the protein sequence information. The present study explored the relationship between sequence complexity and structural fractal dimension, secondary structure information, number of domains and also kinetic parameters considering several methodologies. Our results indicate that some sequence complexity indexes are sensitive enough to differentiate native from random sequences, even when the differences are small. We also found that proteins with increased complexity present a higher number of domains, increased length and mean solvent accessibility. Moreover, proteins with lower complexity revealed an increased folding and unfolding constant rate. Interestingly, we found a significant correlation between protein sequence complexity and structural fractal dimension and a significant effect of the secondary structure classes.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 15