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Prediction of the initial folding sites and the entire folding processes for Ig‐like beta‐sandwich proteins
Author(s) -
Aumpuchin Panyavut,
Hamaue Shoya,
Kikuchi Takeshi
Publication year - 2020
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25862
Subject(s) - protein folding , phi value analysis , folding (dsp implementation) , protein structure prediction , contact order , computational biology , protein structure , native state , sequence (biology) , peptide sequence , downhill folding , chemistry , titin , crystallography , biology , biochemistry , microbiology and biotechnology , engineering , gene , electrical engineering , sarcomere , myocyte
Describing the whole story of protein folding is currently the main enigmatic problem in molecular bioinformatics study. Protein folding mechanisms have been intensively investigated with experimental as well as simulation techniques. Since a protein folds into its specific 3D structure from a unique amino acid sequence, it is interesting to extract as much information as possible from the amino acid sequence of a protein. Analyses based on inter‐residue average distance statistics and a coarse‐grained Gō‐model simulation were conducted on Ig and FN3 domains of a titin protein to decode the folding mechanisms from their sequence data and native structure data, respectively. The central region of all domains was predicted to be an initial folding unit, that is, stable in an early state of folding. This common feature coincides well with the experimental results and underscores the significance of the β‐sandwich proteins' common structure, namely, the key strands for folding and the Greek‐key motif, which is located in the central region. We confirmed that our sequence‐based techniques were able to predict the initial folding event just next to the denatured state and that a 3D‐based Gō‐model simulation can be used to investigate the whole process of protein folding.

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