structural-biology-std-aids-2018-scientifictracks

Page 25

Note:

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

allied

academies

STD-AIDS AND INFECTIOUS DISEASES

STRUCTURAL BIOLOGY AND PROTEOMICS

International Conference on

Joint Event on

Panyavut Aumpuchin et al., J Genet Mol Biol 2018, Volume 2

THE FOLDING MECHANISMS PREDICTION

OF IG-LIKE BETA SANDWICH PROTEINS

BASED ON INTER-RESIDUE AVERAGE

DISTANCE STATISTICS METHODS

Panyavut Aumpuchin

and

Takeshi Kikuchi

Ritsumeikan University, Japan

o understand the folding mechanism of a protein is one of the goals in

bioinformatics study. Nowadays, it is enigmatic and difficult to extract

the folding information from its amino acid sequence by using standard

bioinformatics techniques or even experimental protocol which cost and

time consuming. To overcome these problems, we aim to extract the initial

folding unit for titin protein (Ig and fnIII domains) in the mean of inter-residue

average distance statistics, average distance map (ADM) and contact

frequency analysis (F-value). TI I27 and TNfn3 domains are represented for

Ig-domain and fnIII-domain, respectively. Beta-strand two, three, five and six

are significant for the initial folding processes of TI I27. On the other hands,

the central strands of TNfn3 were predicted as a primary folding segment.

Furthermore, known 3D structure and unknown 3D structure domains were

investigated by structure or non-structure basedmultiple sequence alignment,

respectively, to seek the conservation hydrophobic residue and predicted

compact region through the evolution. Our results show well corresponded to

experimental data, phi-value and protection factor of H-D exchange manner.

It is confirming the significance of conserved hydrophobic residues near

F-value peaks for structural stability by using hydrophobic packing. Again, our

prediction methods could extract the folding mechanism by only its amino

acid sequence.

Panyavut Aumpuchin has completed his master’s

degree in the field of Molecular Plant Pathology from

Kasetsart University, Thailand. He is the PhD student

of faculty of Life Sciences, Ritsumeikan University,

Japan.

BIOGRAPHY