作者: E. Tejera , J. Nieto-Villar , I. Rebelo
DOI: 10.1016/J.PHYSA.2014.05.019
关键词: Fractal dimension 、 Mathematics 、 Sequence 、 Biological system 、 Folding (DSP implementation) 、 Correlation 、 Order (biology) 、 Fractal 、 Protein secondary structure 、 Protein sequencing 、 Discrete mathematics
摘要: Abstract The study of protein sequence complexity is not a new area and several methodological approaches are available in order to describe or represent the information. present explored relationship between structural fractal dimension, secondary structure information, number domains also kinetic parameters considering methodologies. Our results indicate that some indexes sensitive enough differentiate native from random sequences, even when differences small. We found proteins with increased higher domains, length mean solvent accessibility. Moreover, lower revealed an folding unfolding constant rate. Interestingly, we significant correlation dimension effect classes.