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Structural Biology 2018 & STD AIDS 2018 Journal of Genetics and Molecular Biology | Volume 2
S e p t e m b e r 0 3 - 0 4 , 2 0 1 8 | B a n g k o k , T h a i l a n d
alliedacademies
STD-AIDS AND INFECTIOUS DISEASES
STRUCTURAL BIOLOGY AND PROTEOMICS
&
International Conference on
International Conference on
Joint Event on
Risako Kimura et al., J Genet Mol Biol 2018, Volume 2
PREDICTION OF FOLDING SITES OF
Β-TREFOIL PROTEINS WITH IRREGULAR
STRUCTURES
Risako Kimura and Takeshi Kikuchi
Ritsumeikan University, Japan
Details of protein folding mechanism are still unknown. The solution to
this problem is useful for elucidating the mechanism and treatment of
diseases caused by misfolding. The relationship between the amino acid
sequence and the structure of a protein is generally thought to be higher
in structural similarity between proteins with high amino acid sequence
identity. However, β-trefoil proteins are known to have a similar structure
despite its low sequence identity among super families. In this study, we
aim to obtain information on protein folding, targeting β-trefoil protein with
a characteristic structure. We already clarified that the central unit is a
folding core in β-trefoil protein with high structural symmetry in the previous.
In this study, we predicted folding cores for β-trefoil proteins with irregular
structures. The compact areas are predicted using a contact map based on
inter-residue average distance statistics (average distance map). Then, high
interaction residues are predicted by F-value analysis which calculates the
contact frequency by using an effective potential derived from inter-residue
average distance statistics. From these, we identify the points important in
forming the 3D structure along given sequence. We also investigated the
conservation of hydrophobic residues among sequences and attempted
to clarify residues important for folding of β-trefoil proteins. Furthermore,
the folding mechanisms of the β-trefoil proteins are simulated using the
Go model and compared it with the obtained results by ADMs. Because of
the ADM analyses, compact regions are found in the N-terminal unit and
the C-terminal unit in a β-trefoil protein treated in this study. In the result of
the F-value analyses, there is a peak of F-value plot in the central unit. After
formation of units at both ends folding occurred, suggesting that the central
unit interacts with them. Similar results were obtained in the results of the Go
model simulations.
Risako Kimura has completed her Bachelor of Sci-
ence from Ritsumeikan University, Japan. Currently,
she is a graduate student of Bioinformatics course of
Advanced Life Sciences from Ritsumeikan University,
Japan.
BIOGRAPHY