Journal of Proteomics & Bioinformatics
Open Access

Takuya Kirioka

Publications

• Research Article
  Detection of Folding Sites of β-Trefoil Fold Proteins Based on Amino Acid Sequence Analyses and Structure-Based Sequence Alignment
  Author(s): Takuya Kirioka, Panyavut Aumpuchin and Takeshi Kikuchi Takuya Kirioka, Panyavut Aumpuchin and Takeshi Kikuchi
  
  The information on the 3D structure of a protein including its folding mechanism is encoded in its amino acid sequence. A β-trefoil protein is well known to have a remarkable 3D structure property, that is, the pseudo three-fold symmetry without clear hydrophobic packing. It is interesting to investigate how information on the folding mechanism to form such a topology is encoded in the amino acid sequence of a protein. In this study, analyses based on inter-residue average distance statistics and the conservation of hydrophobic residues are performed for sequences of 26 β-trefoil proteins to identify significant sites for the initial folding. Results are compared with the native 3D structures. The conserved hydrophobic residues are defined by multiple sequence alignment based on the 3D structures. It is confirmed that a conserved hydrophobic residue is always located in a &b.. View More»
  DOI: 10.4172/jpb.1000446

  Abstract PDF

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